Enzyme Nomenclature

EC 2.4.2

Pentosyltransferases

Continued from EC 2.4.1.301 to EC 2.4.1.347

Contents

EC 2.4.2.1 purine-nucleoside phosphorylase
EC 2.4.2.2 pyrimidine-nucleoside phosphorylase
EC 2.4.2.3 uridine phosphorylase
EC 2.4.2.4 thymidine phosphorylase
EC 2.4.2.5 nucleoside ribosyltransferase
EC 2.4.2.6 nucleoside deoxyribosyltransferase
EC 2.4.2.7 adenine phosphoribosyltransferase
EC 2.4.2.8 hypoxanthine phosphoribosyltransferase
EC 2.4.2.9 uracil phosphoribosyltransferase
EC 2.4.2.10 orotate phosphoribosyltransferase
EC 2.4.2.11 nicotinate phosphoribosyltransferase
EC 2.4.2.12 nicotinamide phosphoribosyltransferase
EC 2.4.2.13 now EC 2.5.1.6
EC 2.4.2.14 amidophosphoribosyltransferase
EC 2.4.2.15 guanosine phosphorylase
EC 2.4.2.16 urate-ribonucleotide phosphorylase
EC 2.4.2.17 ATP phosphoribosyltransferase
EC 2.4.2.18 anthranilate phosphoribosyltransferase
EC 2.4.2.19 nicotinate-nucleotide diphosphorylase (carboxylating)
EC 2.4.2.20 dioxotetrahydropyrimidine phosphoribosyltransferase
EC 2.4.2.21 nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase
EC 2.4.2.22 xanthine phosphoribosyltransferase
EC 2.4.2.23 transferred now covered by EC 2.4.2.2, EC 2.4.2.3 and EC 2.4.2.4
EC 2.4.2.24 1,4-β-D-xylan synthase
EC 2.4.2.25 flavone apiosyltransferase
EC 2.4.2.26 protein xylosyltransferase
EC 2.4.2.27 dTDP-dihydrostreptose—streptidine-6-phosphate dihydrostreptosyltransferase
EC 2.4.2.28 S-methylthio-5'-adenosine phosphorylase
EC 2.4.2.29 tRNA-guanosine34 transglycosylase
EC 2.4.2.30 NAD+ ADP-ribosyltransferase
EC 2.4.2.31 NAD+—protein-arginine ADP-ribosyltransferase
EC 2.4.2.32 dolichyl-phosphate D-xylosyltransferase
EC 2.4.2.33 dolichyl-xylosyl-phosphate—protein xylosyltransferase
EC 2.4.2.34 indolylacetylinositol arabinosyltransferase
EC 2.4.2.35 flavonol-3-O-glycoside xylosyltransferase
EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase
EC 2.4.2.37 NAD+—dinitrogen-reductase ADP-D-ribosyltransferase
EC 2.4.2.38 glycoprotein 2-β-D-xylosyltransferase
EC 2.4.2.39 xyloglucan 6-xylosyltransferase
EC 2.4.2.40 zeatin O-β-D-xylosyltransferase
EC 2.4.2.41 xylogalacturonan β-1,3-xylosyltransferase
EC 2.4.2.42 UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
EC 2.4.2.43 lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
EC 2.4.2.44 S-methyl-5'-thioinosine phosphorylase
EC 2.4.2.45 decaprenyl-phosphate phosphoribosyltransferase
EC 2.4.2.46 galactan 5-O-arabinofuranosyltransferase
EC 2.4.2.47 arabinofuranan 3-O-arabinosyltransferase
EC 2.4.2.48 tRNA-guanine15 transglycosylase
EC 2.4.2.49 neamine phosphoribosyltransferase
EC 2.4.2.50 cyanidin 3-O-galactoside 2''-O-xylosyltransferase
EC 2.4.2.51 anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
EC 2.4.2.52 triphosphoribosyl-dephospho-CoA synthase
EC 2.4.2.53 undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
EC 2.4.2.54 β-ribofuranosylaminobenzene 5'-phosphate synthase
EC 2.4.2.55 nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase
EC 2.4.2.56 kaempferol 3-O-xylosyltransferase
EC 2.4.2.57 AMP phosphorylase
EC 2.4.2.58 hydroxyproline O-arabinosyltransferase

Entries

EC 2.4.2.1

Accepted name: purine-nucleoside phosphorylase

Reaction: (1) purine ribonucleoside + phosphate = purine + α-D-ribose 1-phosphate
(2) purine 2'-deoxyribonucleoside + phosphate = purine + 2-deoxy-α-D-ribose 1-phosphate

Other name(s): inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase

Systematic name: purine-nucleoside:phosphate ribosyltransferase

Comments: Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-21-1

References:

1. Agarwal, R.P. and Parks, R.E. Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties. J. Biol. Chem. 244 (1969) 644-647. [PMID: 69183117]

2. Friedkin, M. and Kalckar, H. Nucleoside phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 5, Academic Press, New York, 1961, p. 237-255.

3. Heppel, L.A. and Hilmoe, R.J. Phosphorolysis and hydrolysis of purine ribosides from yeast. J. Biol. Chem. 198 (1952) 683-694.

4. Kalckar, H.M. The enzymatic synthesis of purine ribosides. J. Biol. Chem. 167 (1947) 477-486.

5. Saunders, P.P., Wilson, B.A. and Saunders, G.F. Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J. Biol. Chem. 244 (1969) 3691-3697. [PMID: 4978445].

6. Tsuboi, K.K. and Hudson, P.B. Enzymes of the human erythrocyte. I. Purine nucleoside phosphorylase; isolation procedure. J. Biol. Chem. 224 (1957) 879-887.

[EC 2.4.2.1 created 1961]

EC 2.4.2.2

Accepted name: pyrimidine-nucleoside phosphorylase

Reaction: (1) uridine + phosphate = uracil + α-D-ribose 1-phosphate
(2) thymidine + phosphate = thymine + 2-deoxy-α-D-ribose 1-phosphate
(3) 2'-deoxyuridine + phosphate = uracil + 2-deoxy-α-D-ribose 1-phosphate

Other name(s): Py-NPase; pdp (gene name)

Systematic name: pyrimidine-nucleoside:phosphate (2'-deoxy)-α-D-ribosyltransferase

Comments: Unlike EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine [3]. The reaction is reversible, and the enzyme does not distinguish between α-D-ribose 1-phosphate and 2'-deoxy-α-D-ribose 1-phosphate in the synthetic direction.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9055-35-0

References:

1. Friedkin, M. and Kalckar, H. Nucleoside phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 237-255.

2. Saunders, P.P., Wilson, B.A. and Saunders, G.F. Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J. Biol. Chem. 244 (1969) 3691-3697. [PMID: 4978445]

3. Hamamoto, T., Noguchi, T. and Midorikawa, Y. Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2. Biosci. Biotechnol. Biochem. 60 (1996) 1179-1180. [PMID: 8782414]

4. Okuyama, K., Hamamoto, T., Noguchi, T. and Midorikawa, Y. Molecular cloning and expression of the pyrimidine nucleoside phosphorylase gene from Bacillus stearothermophilus TH 6-2. Biosci. Biotechnol. Biochem. 60 (1996) 1655-1659. [PMID: 8987664]

5. Pugmire, M.J. and Ealick, S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure 6 (1998) 1467-1479. [PMID: 9817849]

[EC 2.4.2.2 created 1961, modified 2013]

EC 2.4.2.3

Accepted name: uridine phosphorylase

Reaction: uridine + phosphate = uracil + α-D-ribose 1-phosphate

Other name(s): pyrimidine phosphorylase; UrdPase; UPH; UPase

Systematic name: uridine:phosphate α-D-ribosyltransferase

Comments: The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-22-2

References:

1. Canellakis, E.S. Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism. J. Biol. Chem. 227 (1957) 329-338.

2. Paege, L.M. and Schlenk, F. Bacterial uracil riboside phosphorylase. Arch. Biochem. Biophys. 40 (1952) 42-49.

3. Pontis, H., Degerstedt, G. and Reichard, P. Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor. Biochim. Biophys. Acta 51 (1961) 138-147.

4. Pontis, H., Degerstedt, G. and Reichard, P. Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor. Biochim. Biophys. Acta 51 (1961) 138-147. [PMID: 13737038]

5. Watanabe, S. and Uchida, T. Cloning and expression of human uridine phosphorylase. Biochem. Biophys. Res. Commun. 216 (1995) 265-272. [PMID: 7488099]

6. Liu, M., Cao, D., Russell, R., Handschumacher, R.E. and Pizzorno, G. Expression, characterization, and detection of human uridine phosphorylase and identification of variant uridine phosphorolytic activity in selected human tumors. Cancer Res. 58 (1998) 5418-5424. [PMID: 9850074]

[EC 2.4.2.3 created 1961]

EC 2.4.2.4

Accepted name: thymidine phosphorylase

Reaction: thymidine + phosphate = thymine + 2-deoxy-α-D-ribose 1-phosphate

Other name(s): pyrimidine phosphorylase; thymidine-orthophosphate deoxyribosyltransferase; animal growth regulators, blood platelet-derived endothelial cell growth factors; blood platelet-derived endothelial cell growth factor; deoxythymidine phosphorylase; gliostatins; pyrimidine deoxynucleoside phosphorylase; thymidine:phosphate deoxy-D-ribosyltransferase

Systematic name: thymidine:phosphate deoxy-α-D-ribosyltransferase

Comments: The enzyme in some tissues also catalyses deoxyribosyltransferase reactions of the type catalysed by EC 2.4.2.6, nucleoside deoxyribosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-23-3

References:

1. Friedkin, M. and Roberts, D. The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase in mammalian tissue. J. Biol. Chem. 207 (1954) 245-256.

2. Zimmerman, M. and Seidenberg, J. Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues. J. Biol. Chem. 239 (1964) 2618-2621.

3. Zimmerman, M. Deoxyribosyl transfer. II. Nucleoside:pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases. J. Biol. Chem. 239 (1964) 2622-2627.

[EC 2.4.2.4 created 1961]

EC 2.4.2.5

Accepted name: nucleoside ribosyltransferase

Reaction: D-ribosyl-base1 + base2 = D-ribosyl-base2 + base1

Other name(s): nucleoside N-ribosyltransferase

Systematic name: nucleoside:purine(pyrimidine) D-ribosyltransferase

Comments: Base1 and base2 represent various purines and pyrimidines.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-31-3

References:

1. Koch, A.L. Some enzymes of nucleoside metabolism of Escherichia coli. J. Biol. Chem. 223 (1956) 535-549.

[EC 2.4.2.5 created 1961]

EC 2.4.2.6

Accepted name: nucleoside deoxyribosyltransferase

Reaction: 2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1

Other name(s): purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase; deoxyribose transferase; nucleoside trans-N-deoxyribosylase; trans-deoxyribosylase; trans-N-deoxyribosylase; trans-N-glycosidase; nucleoside deoxyribosyltransferase I (purine nucleoside:purine deoxyribosyltransferase: strictly specific for transfer between purine bases); nucleoside deoxyribosyltransferase II [purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyltransferase]

Systematic name: nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase

Comments: Base1 and base2 represent various purines and pyrimidines.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-86-2

References:

1. Kalckar, H.M., MacNutt, W.S. and Hoff-Jørgensen, E. Trans-N-glycosidase studied with radioactive adenine. Biochem. J. 50 (1952) 397-400.

2. MacNutt, W.S. The enzymically catalysed transfer of the deoxyribosyl group from one purine or pyrimidine to another. Biochem. J. 50 (1952) 384-397.

3. Roush, A.H. and Betz, R.F. Purification and properties of trans-N-deoxyribosylase. J. Biol. Chem. 233 (1958) 261-266.

[EC 2.4.2.6 created 1961]

EC 2.4.2.7

Accepted name: adenine phosphoribosyltransferase

Reaction: AMP + diphosphate = adenine + 5-phospho-α-D-ribose 1-diphosphate

For diagram of reaction click here.

Other name(s): AMP pyrophosphorylase; transphosphoribosidase; APRT; AMP-pyrophosphate phosphoribosyltransferase; adenine phosphoribosylpyrophosphate transferase; adenosine phosphoribosyltransferase; adenylate pyrophosphorylase; adenylic pyrophosphorylase

Systematic name: AMP:diphosphate phospho-D-ribosyltransferase

Comments: 5-Amino-4-imidazolecarboxamide can replace adenine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-80-9

References:

1. Flaks, J.G., Erwin, M.J. and Buchanan, J.M. Biosynthesis of the purines. XVI. The synthesis of adenosine 5'-phosphate and 5-amino-4-imidazolecarboxamide ribotide by a nucleotide pyrophosphorylase. J. Biol. Chem. 228 (1957) 201-213.

2. Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417-427.

3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.

[EC 2.4.2.7 created 1961]

EC 2.4.2.8

Accepted name: hypoxanthine phosphoribosyltransferase

Reaction: IMP + diphosphate = hypoxanthine + 5-phospho-α-D-ribose 1-diphosphate

Other name(s): IMP pyrophosphorylase; transphosphoribosidase; hypoxanthine—guanine phosphoribosyltransferase; guanine phosphoribosyltransferase; GPRT; HPRT; guanosine 5'-phosphate pyrophosphorylase; IMP-GMP pyrophosphorylase; HGPRTase; 6-hydroxypurine phosphoribosyltransferase; 6-mercaptopurine phosphoribosyltransferase; GMP pyrophosphorylase; guanine-hypoxanthine phosphoribosyltransferase; guanosine phosphoribosyltransferase; guanylate pyrophosphorylase; guanylic pyrophosphorylase; inosinate pyrophosphorylase; inosine 5'-phosphate pyrophosphorylase; inosinic acid pyrophosphorylase; inosinic pyrophosphorylase; 6-mercaptopurine phosphoribosyltransferase; purine-6-thiol phosphoribosyltransferase

Systematic name: IMP:diphosphate phospho-D-ribosyltransferase

Comments: Guanine and 6-mercaptopurine can replace hypoxanthine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9016-12-0

References:

1. Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136-158.

2. Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417-427.

3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.

4. Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885-895.

[EC 2.4.2.8 created 1961, modified 1982]

EC 2.4.2.9

Accepted name: uracil phosphoribosyltransferase

Reaction: UMP + diphosphate = uracil + 5-phospho-α-D-ribose 1-diphosphate

Other name(s): UMP pyrophosphorylase; UPRTase; UMP:pyrophosphate phosphoribosyltransferase; uridine 5'-phosphate pyrophosphorylase; uridine monophosphate pyrophosphorylase; uridylate pyrophosphorylase; uridylic pyrophosphorylase

Systematic name: UMP:diphosphate phospho-α-D-ribosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-24-4

References:

1. Crawford, I., Kornberg, A. and Simms, E.S. Conversion of uracil and orotate to uridine 5'-phosphate by enzymes in lactobacilli. J. Biol. Chem. 226 (1967) 1093-1101.

2. Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136-158.

[EC 2.4.2.9 created 1961]

EC 2.4.2.10

Accepted name: orotate phosphoribosyltransferase

Reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-α-D-ribose 1-diphosphate

For diagram click here.

Other name(s): orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase

Systematic name: orotidine-5'-phosphate:diphosphate phospho-α-D-ribosyl-transferase

Comments: The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-25-5

References:

1. Jones, M.E., Kavipurapu, P.R. and Traut, T.W. Orotate phosphoribosyltransferase: orotidylate decarboxylase (Ehrlich ascites cell). Methods Enzymol. 51 (1978) 155-167. [PMID: 692383]

2. Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of pyrimidine nucleotides. Orotidine-5'-phosphate and uridine-5'-phosphate. J. Biol. Chem. 215 (1955) 403-415.

3. McClard, R.W., Black, M.J., Livingstone, L.R. and Jones, M.E. Isolation and initial characterization of the single polypeptide that synthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthase. Biochemistry 19 (1980) 4699-4706. [PMID: 6893554]

[EC 2.4.2.10 created 1961, modified 1986]

[EC 2.4.2.11 Transferred entry: EC 2.4.2.11, nicotinate phosphoribosyltransferase. Now EC 6.3.4.21 nicotinate phosphoribosyltransferase. (EC 2.4.2.11 created 1961, deleted 2013)]

EC 2.4.2.12

Accepted name: nicotinamide phosphoribosyltransferase

Reaction: nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-α-D-ribose 1-diphosphate

For diagram of reaction click here.

Other name(s): NMN pyrophosphorylase; nicotinamide mononucleotide pyrophosphorylase; nicotinamide mononucleotide synthetase; NMN synthetase; nicotinamide-nucleotide:diphosphate phospho-α-D-ribosyltransferase

Systematic name: nicotinamide-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-27-7

References:

1. Preiss, J. and Handler, P. Enzymatic synthesis of nicotinamide mononucleotide. J. Biol. Chem. 225 (1957) 759-770.

[EC 2.4.2.12 created 1961]

[EC 2.4.2.13 Transferred entry: now EC 2.5.1.6 methionine adenosyltransferase (EC 2.4.2.13 created 1961, deleted 1965)]

EC 2.4.2.14

Accepted name: amidophosphoribosyltransferase

Reaction: 5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-α-D-ribose 1-diphosphate + H2O

For diagram click here.

Other name(s): phosphoribosyldiphosphate 5-amidotransferase; glutamine phosphoribosyldiphosphate amidotransferase; α-5-phosphoribosyl-1-pyrophosphate amidotransferase; 5′-phosphoribosylpyrophosphate amidotransferase; 5-phosphoribosyl-1-pyrophosphate amidotransferase; 5-phosphororibosyl-1-pyrophosphate amidotransferase; glutamine 5-phosphoribosylpyrophosphate amidotransferase; glutamine ribosylpyrophosphate 5-phosphate amidotransferase; phosphoribose pyrophosphate amidotransferase; phosphoribosyl pyrophosphate amidotransferase; phosphoribosylpyrophosphate glutamyl amidotransferase; 5-phosphoribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating)

Systematic name: 5-phospho-β-D-ribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-82-7

References:

1. Caskey, C.T., Ashton, D.M. and Wyngaarden, J.B. The enzymology of feedback inhibition of glutamine phosphoribosylpyrophosphate amidotransferase by purine ribonucleotides. J. Biol. Chem. 239 (1964) 2570-2579.

2. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXI. 5-Phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 233 (1958) 451-455.

[EC 2.4.2.14 created 1961]

EC 2.4.2.15

Accepted name: guanosine phosphorylase

Reaction: guanosine + phosphate = guanine + α-D-ribose 1-phosphate

Other Name(s): guanosine:phosphate D-ribosyltransferase

Systematic name: guanosine:phosphate α-D-ribosyltransferase

Comments: Also acts on deoxyguanosine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9030-28-8

References:

1. Yamada, E.W. The phosphorolysis of nucleosides by rabbit bone marrow. J. Biol. Chem. 236 (1961) 3043-3046.

[EC 2.4.2.15 created 1965]

EC 2.4.2.16

Accepted name: urate-ribonucleotide phosphorylase

Reaction: urate D-ribonucleotide + phosphate = urate + α-D-ribose 1-phosphate

Other name(s): UAR phosphorylase; urate-ribonucleotide:phosphate D-ribosyltransferase; urate-ribonucleotide:phosphate α-D-ribosyltransferase

Systematic name: urate-D-ribonucleotide:phosphate α-D-ribosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-29-9

References:

1. Laster, L. and Blair, A. An intestinal phosphorylase for uric acid ribonucleoside. J. Biol. Chem. 238 (1963) 3348-3357.

[EC 2.4.2.16 created 1965]

EC 2.4.2.17

Accepted name: ATP phosphoribosyltransferase

Reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-α-D-ribose 1-diphosphate

For diagram click here.

Other name(s): phosphoribosyl-ATP pyrophosphorylase; adenosine triphosphate phosphoribosyltransferase; phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase; phosphoribosyl ATP synthetase; phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase; phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase; phosphoribosyladenosine triphosphate pyrophosphorylase; phosphoribosyladenosine triphosphate synthetase; 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase

Systematic name: 1-(5-phospho-β-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase

Comments: Involved in histidine biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-46-3

References:

1. Ames, B.N., Martin, R.G. and Garry, B.J. The first step of histidine biosynthesis. J. Biol. Chem. 236 (1961) 2019-2026.

2. Martin, R.G. The phosphorolysis of nucleosides by rabbit bone marrow: The nature of feedback inhibition by histidine. J. Biol. Chem. 238 (1963) 257-268.

3. Voll, M.J., Appella, E. and Martin, R.G. Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis. J. Biol. Chem. 242 (1967) 1760-1767. [PMID: 5337591]

[EC 2.4.2.17 created 1972]

EC 2.4.2.18

Accepted name: anthranilate phosphoribosyltransferase

Reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-α-D-ribose 1-diphosphate

For diagram click here.

Other name(s): phosphoribosyl-anthranilate pyrophosphorylase; PRT; anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase; anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase; phosphoribosylanthranilate pyrophosphorylase; phosphoribosylanthranilate transferase; anthranilate-PP-ribose-P phosphoribosyltransferase

Systematic name: N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-α-D-ribosyltransferase

Comments: In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9059-35-2

References:

1. Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365-380.

2. Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55-77.

3. Ito, J. and Yanofsky, C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J. Bacteriol. 97 (1969) 734-742.

4. Wegman, J. and DeMoss, J.A. The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa. J. Biol. Chem. 240 (1965) 3781-3788. [PMID: 5842052]

[EC 2.4.2.18 created 1972]

EC 2.4.2.19

Accepted name: nicotinate-nucleotide diphosphorylase (carboxylating)

Reaction: nicotinate β-D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-α-D-ribose 1-diphosphate

For diagram of reaction click here.

Other name(s): quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase; nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)

Systematic name: nicotinate-β-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)

Comments: This is the first enzyme that prokaryotes and eukaryotes have in common in the production of NAD+ as some prokaryotes use an L-aspartate pathway to produce quinolinate whereas all eukaryotes use tryptophan as the starting material [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37277-74-0

References:

1. Gholson, R.K., Ueda, I., Ogasawara, N. and Henderson, L.M. The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver. J. Biol. Chem. 239 (1964) 1208-1214.

2. Packman, P.M. and Jakoby, W.B. Crystalline quinolinate phosphoribosyltransferase. J. Biol. Chem. 240 (1965) 4107-4108. [PMID: 5320648]

3. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851857. [PMID: 16698895]

[EC 2.4.2.19 created 1972]

EC 2.4.2.20

Accepted name: dioxotetrahydropyrimidine phosphoribosyltransferase

Reaction: A 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = a 2,4-dioxotetrahydropyrimidine + 5-phospho-α-D-ribose 1-diphosphate

Other name(s): dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase; dioxotetrahydropyrimidine phosphoribosyl transferase; dioxotetrahydropyrimidine ribonucleotide pyrophosphorylase; 2,4-dioxotetrahydropyrimidine-nucleotide:diphosphate phospho-α-D-ribosyltransferase

Systematic name: 2,4-dioxotetrahydropyrimidine-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase

Comments: Acts (in the reverse direction) on uracil and other pyrimidines and pteridines containing a 2,4-diketo structure.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-75-1

References:

1. Hatfield, D. and Wyngaarden, J.B. 3-Ribosylpurines. I. Synthesis of (3-ribosyluric acid) 5'-phosphate and (3-ribosylxanthine) 5'-phosphate by a pyrimidine ribonucleotide pyrophosphorylase of beef erythrocytes. J. Biol. Chem. 239 (1964) 2580-2586.

[EC 2.4.2.20 created 1972]

EC 2.4.2.21

Accepted name: nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase

Reaction: β-nicotinate D-ribonucleotide + dimethylbenzimidazole = nicotinate + N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole

For diagram click here.

Glossary: α-ribazole 5′-phosphate = N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole

Other name(s): nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase; nicotinate ribonucleotide:benzimidazole (adenine) phosphoribosyltransferase; nicotinate-nucleotide:dimethylbenzimidazole phospho-D-ribosyltransferase; CobT; nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole phosphoribosyltransferase

Systematic name: nicotinate-nucleotide:5,6-dimethylbenzimidazole phospho-D-ribosyltransferase

Comments: Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-α-D-ribosyladenine 5'-phosphate. The product of the reaction, α-ribazole 5′-phosphate, forms part of the corrin-biosynthesis pathway and is a substrate for EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase [4]. It can also be dephosphorylated to form α-ribazole by the action of EC 3.1.3.73, α-ribazole phosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37277-76-2

References:

1. Friedmann, H.C. Partial purification and properties of a single displacement trans-N-glycosidase. J. Biol. Chem. 240 (1965) 413-418. [PMID: 14253445]

2. Friedmann, H.C. and Fyfe, J.A. Pseudovitamin B12 biosynthesis. Enzymatic formation of a new adenylic acid, 7-α-D-ribofuranosyladenine 5'-phosphate. J. Biol. Chem. 244 (1969) 1667-1671. [PMID: 5780835]

3. Fyfe, J.A. and Friedmann, H.C. Vitamin B12 biosynthesis. Enzyme studies on the formation of the α-glycosidic nucleotide precursor. J. Biol. Chem. 244 (1969) 1659-1666. [PMID: 4238408]

4. Cameron, B., Blanche, F., Rouyez, M.C., Bisch, D., Famechon, A., Couder, M., Cauchois, L., Thibaut, D., Debussche, L. and Crouzet, J. Genetic analysis, nucleotide sequence, and products of two Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide: dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5′-phosphate) synthase. J. Bacteriol. 173 (1991) 6066-;6073. [PMID: 1917841]

5. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica. J. Biol. Chem. 276 (2001) 37612-37620. [PMID: 11441022]

6. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Capture of a labile substrate by expulsion of water molecules from the active site of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella enterica. J. Biol. Chem. 277 (2002) 41120-41127. [PMID: 12101181]

[EC 2.4.2.21 created 1972]

EC 2.4.2.22

Accepted name: xanthine phosphoribosyltransferase

Reaction: XMP + diphosphate = 5-phospho-α-D-ribose 1-diphosphate + xanthine

Glossary: XMP = 9-(5-phospho-β-D-ribosyl)xanthine = xanthosine 5'-monophosphate

Other name(s): Xan phosphoribosyltransferase; xanthosine 5'-phosphate pyrophosphorylase; xanthylate pyrophosphorylase; xanthylic pyrophosphorylase; XMP pyrophosphorylase; 5-phospho-α-D-ribose-1-diphosphate:xanthine phospho-D-ribosyltransferase; 9-(5-phospho-β-D-ribosyl)xanthine:diphosphate 5-phospho-α-D-ribosyltransferase

Systematic name: XMP:diphosphate 5-phospho-α-D-ribosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-10-3

References:

1. Krenitsky, T.A., Neil, S.M. and Miller, R.L. Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities. J. Biol. Chem. 245 (1970) 2605-2611. [PMID: 4910918]

[EC 2.4.2.22 created 1972]

[EC 2.4.2.23 Transferred entry: deoxyuridine phosphorylase. This activity has been shown to be catalysed by EC 2.4.2.2, pyrimidine-nucleoside phosphorylase, EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase. (EC 2.4.2.23 created 1972, deleted 2013)]

EC 2.4.2.24

Accepted name: 1,4-β-D-xylan synthase

Reaction: UDP-D-xylose + [(1→4)-β-D-xylan]n = UDP + [(1→4)-β-D-xylan]n+1

Other name(s): uridine diphosphoxylose-1,4-β-xylan xylosyltransferase; 1,4-β-xylan synthase; xylan synthase; xylan synthetase

Systematic name: UDP-D-xylose:1,4-β-D-xylan 4-β-D-xylosyltransferase

Comments: Formerly EC 2.4.1.72.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-73-9

References:

1. Bailey, R.W. and Hassid, W.Z. Xylan synthesis from uridine-diphosphate-D-xylose by particulate preparations from immature corncobs. Proc. Natl. Acad. Sci. USA 56 (1966) 1586-1593.

[EC 2.4.2.24 created 1972 as EC 2.4.1.72, transferred 1976 to EC 2.4.2.24]

EC 2.4.2.25

Accepted name: flavone apiosyltransferase

Reaction: UDP-α-D-apiose + apigenin 7-O-β-D-glucoside = UDP + apigenin 7-O-[β-D-apiosyl-(1→2)-β-D-glucoside]

For diagram click here.

Glossary: apigenin = 5,4',7-trihydroxyflavone
β-D-apiose = (2R,3R,4R)-4-(hydroxymethyl)tetrahydrofuran-2,3,4-triol

Other name(s): uridine diphosphoapiose-flavone apiosyltransferase; UDP-apiose:7-O-(β-D-glucosyl)-flavone apiosyltransferase; UDP-apiose:5,4'-dihydroxyflavone 7-O-β-D-glucoside 2"-O-β-D-apiofuranosyltransferase

Systematic name: UDP-apiose:4',5-dihydroxyflavone 7-O-β-D-glucoside 2"-O-β-D-apiofuranosyltransferase

Comments: 7-O-β-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37332-49-3

References:

1. Ortmann, R., Sutter, A. and Grisebach, H. Purification and properties of UDPapiose: 7-O-(β-D-glucosyl)-flavone apiosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 289 (1972) 293-302. [PMID: 4650134]

[EC 2.4.2.25 created 1976]

EC 2.4.2.26

Accepted name: protein xylosyltransferase

Reaction: UDP-α-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(β-D-xylosyl)-L-serine

For diagram of reaction click here

Other name(s): UDP-D-xylose:core protein β-D-xylosyltransferase; UDP-D-xylose:core protein xylosyltransferase; UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase; UDP-xylose-core protein β-D-xylosyltransferase; uridine diphosphoxylose-core protein β-xylosyltransferase; uridine diphosphoxylose-protein xylosyltransferase; UDP-D-xylose:protein β-D-xylosyltransferase

Systematic name: UDP-α-D-xylose:protein β-D-xylosyltransferase (configuration-inverting)

Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55576-38-0

References:

1. Stoolmiller, A.C., Horwitz, A.L. and Dorfman, A. Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase. J. Biol. Chem. 247 (1972) 3525-3532. [PMID: 5030630]

2. Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304 (2000) 517-528. [PMID: 11099377]

[EC 2.4.2.26 created 1976, modified 2002, modified 2016]

EC 2.4.2.27

Accepted name: dTDP-dihydrostreptose—streptidine-6-phosphate dihydrostreptosyltransferase

Reaction: dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + O-(1→4)-α-L-dihydrostreptosyl-streptidine 6-phosphate

Other name(s): thymidine diphosphodihydrostreptose-streptidine 6-phosphate dihydrostreptosyltransferase

Systematic name: dTDP-L-dihydrostreptose:streptidine-6-phosphate dihydrostreptosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73699-20-4

References:

1. Kniep, B. and Grisebach, H. Biosynthesis of streptomycin. Purification and properties of a dTDP-L-dihydrostreptose: streptidine-6-phosphate dihydrostreptosyltransferase from Streptomyces griseus.Eur. J. Biochem. 105 (1980) 139-144. [PMID: 6768553]

[EC 2.4.2.27 created 1982]

EC 2.4.2.28

Accepted name: S-methyl-5'-thioadenosine phosphorylase

Reaction: S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-α-D-ribose 1-phosphate

For diagram click here

Other name(s): 5′-deoxy-5′-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5′-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase

Systematic name: S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase

Comments: Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 61970-06-7

References:

1. Carteni-Farina, M., Oliva, A., Romeo, G., Napolitano, G., De Rosa, M., Gambacorta, A. and Zappia, V. 5'-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties. Eur. J. Biochem. 101 (1979) 317-324. [PMID: 118001]

2. Garbers, D.L. Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung. Biochim. Biophys. Acta 523 (1978) 82-93. [MPID: 415762]

3. Pegg, A.E. and Williams-Ashman, H.G. Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate. Biochem. J. 115 (1969) 241-247. [PMID: 5378381]

[EC 2.4.2.28 created 1983]

EC 2.4.2.29

Accepted name: tRNA-guanosine34 transglycosylase

Reaction: (1) guanine34 in tRNA + queuine = queuine34 in tRNA + guanine
(2) guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine

For diagram of reaction click here

Glossary: 7-aminomethyl-7-carbaguanine = preQ1 = 7-aminomethyl-7-deazaguanine
7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine
queuine = base Q = 2-amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydropyrrolo[3,2-e]pyrimidin-4-one

Other name(s): guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguous); Q-insertase (ambiguous); queuine34 transfer ribonucleate ribosyltransferase; transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine34 transglycosidase; queuine tRNA-ribosyltransferase (ambiguous); TGT; [tRNA]-guanine34:queuine tRNA-D-ribosyltransferase; transfer ribonucleic acid guanine34 transglycosylase

Systematic name: tRNA-guanosine34:queuine tRNA-D-ribosyltransferase

Comments: Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine [4,5]. The eubacterial enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn [2]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 72162-89-1

References:

1. Howes, N.K. and Farkas, W.R. Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA. J. Biol. Chem. 253 (1978) 9082-9087. [PMID: 721832]

2. Okada, N., Noguchi, S., Kasai, H., Shindo-Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction. J. Biol. Chem. 254 (1979) 3067-3073. [PMID: 372186]

3. Shindo-Okada, N., Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Transfer ribonucleic acid guanine transglycosylase isolated from rat liver. Biochemistry 19 (1980) 395-400. [PMID: 6986171]

4. Todorov, K.A. and Garcia, G.A. Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity. Biochemistry 45 (2006) 617-625. [PMID: 16401090]

5. Boland, C., Hayes, P., Santa-Maria, I., Nishimura, S. and Kelly, V.P. Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase. J. Biol. Chem. 284 (2009) 18218-18227. [PMID: 19414587]

[EC 2.4.2.29 created 1984, modified 2007, modified 2012]

EC 2.4.2.30

Accepted name: NAD+ ADP-ribosyltransferase

Reaction: NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+

For diagram click here.

Other name(s): poly(ADP-ribose) synthase; ADP-ribosyltransferase (polymerizing); NAD ADP-ribosyltransferase; PARP; PARP-1; NAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase (incorrect); NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase

Systematic name: NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase

Comments: The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 58319-92-9

References:

1. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]

2. Ueda, K., Kawaichi, M. and Hayaishi, O. Poly(ADP-ribose) synthetase. In: Hayaishi, O. and Ueda, K. (Eds.), ADP-Ribosylation Reactions: Biology and Medicine, Academic Press, London, 1982, p. 117-155.

3. Ushiro, H., Yokoyama, Y. and Shizuta, Y. Purification and characterization of poly (ADP-ribose) synthetase from human placenta. J. Biol. Chem. 262 (1987) 2352-2357. [PMID: 2434482]

[EC 2.4.2.30 created 1984, modified 1990]

EC 2.4.2.31

Accepted name: NAD+—protein-arginine ADP-ribosyltransferase

Reaction: NAD+ + protein L-arginine = nicotinamide + Nω-(ADP-D-ribosyl)-protein-L-arginine

Other name(s): ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ADP-ribosyltransferase; NAD(P)+:L-arginine ADP-D-ribosyltransferase; mono-ADP-ribosyltransferase; ART; ART1; ART2; ART3; ART4; ART5; ART6; ART7; NAD(P)+—protein-arginine ADP-ribosyltransferase

Systematic name: NAD+:protein-L-arginine ADP-D-ribosyltransferase

Comments: Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nω-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymatic activities. (cf. EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 81457-93-4

References:

1. Moss, J., Stanley, S.J. and Oppenheimer, N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891-8894. [PMID: 225315]

2. Moss, J., Stanley, S.J. and Watkins, P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838-5840. [PMID: 6247348]

3. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]

4. Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953-1958. [PMID: 12727863]

5. Paone, G., Stevens, L.A., Levine, R.L., Bourgeois, C., Steagall, W.K., Gochuico, B.R. and Moss, J. ADP-ribosyltransferase-specific modification of human neutrophil peptide-1. J. Biol. Chem. 281 (2006) 1705417060. [PMID: 16627471]

[EC 2.4.2.31 created 1984, modified 1990, modified 2006]

EC 2.4.2.32

Accepted name: dolichyl-phosphate D-xylosyltransferase

Reaction: UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl phosphate

Glossary: dolichol

Systematic name: UDP-D-xylose:dolichyl-phosphate D-xylosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]

[EC 2.4.2.32 created 1984, modified 2003]

EC 2.4.2.33

Accepted name: dolichyl-xylosyl-phosphate—protein xylosyltransferase

Reaction: dolichyl D-xylosyl phosphate + protein = dolichyl phosphate + D-xylosylprotein

Systematic name: dolichyl-D-xylosyl-phosphate:protein D-xylosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]

[EC 2.4.2.33 created 1984]

EC 2.4.2.34

Accepted name: indolylacetylinositol arabinosyltransferase

Reaction: UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol = UDP + (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside

Other name(s): arabinosylindolylacetylinositol synthase; UDP-L-arabinose:indol-3-ylacetyl-myo-inositol L-arabinosyltransferase; UDP-L-arabinose:(indol-3-yl)acetyl-myo-inositol L-arabinosyltransferase

Systematic name: UDP-L-arabinose:(indol-3-yl)acetyl-1D-myo-inositol L-arabinosyltransferase

Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. For a diagram showing the biosynthesis of UDP-L-arabinose, click here.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84720-96-7

References:

1. Corcuera, L.J. and Bandurski, R.S. Biosynthesis of indol-3-yl-acetyl-myo-inositol arabinoside in kernels of Zea mays L. Plant Physiol. 70 (1982) 1664-1666.

[EC 2.4.2.34 created 1986, modified 2003]

EC 2.4.2.35

Accepted name: flavonol-3-O-glycoside xylosyltransferase

Reaction: UDP-α-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol 3-[β-D-xylosyl-(1→2)-β-D-glycoside]

For diagram of reaction click here.

Other name(s): UDP-D-xylose:flavonol-3-O-glycoside 2''-O-β-D-xylosyltransferase

Systematic name: UDP-α-D-xylose:flavonol-3-O-glycoside 2''-O-β-D-xylosyltransferase

Comments: Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-90-9

References:

1. Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587-599.

[EC 2.4.2.35 created 1986, modified 2014]

EC 2.4.2.36

Accepted name: NAD+—diphthamide ADP-ribosyltransferase

Reaction: NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]

For diagram of reaction click here.

Glossary: diphthamide = 2-[4-amino-4-oxo-3-(trimethylammonio)butyl]-L-histidine

Other name(s): ADP-ribosyltransferase; mono(ADPribosyl)transferase; NAD—diphthamide ADP-ribosyltransferase; NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase

Systematic name: NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase

Comments: Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+—protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52933-21-8

References:

1. Lee, H. and Iglewski, W.J. Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A. Proc. Natl. Acad. Sci. USA 81 (1984) 2703-2707. [PMID: 6326138]

2. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]

[EC 2.4.2.36 created 1990, modified 2013]

EC 2.4.2.37

Accepted name: NAD+—dinitrogen-reductase ADP-D-ribosyltransferase

Reaction: NAD+ + [dinitrogen reductase]-L-arginine = nicotinamide + [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine

Other name(s): NAD-azoferredoxin (ADPribose)transferase; NAD-dinitrogen-reductase ADP-D-ribosyltransferase; draT (gene name)

Systematic name: NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase

Comments: The combined action of this enzyme and EC 3.2.2.24, ADP-ribosyl-[dinitrogen reductase] hydrolase, controls the activity level of nitrogenase (EC 1.18.6.1). In the presence of ammonium, the product of nitrogenase, this enzyme covalently links an ADP-ribose moiety to a specific arginine residue of the dinitrogenase reductase component of nitrogenase, blocking its activity.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117590-45-1

References:

1. Lowery, R.G. and Ludden, P.W. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum. J. Biol. Chem. 263 (1988) 16714-16719. [PMID: 3141411]

2. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218 (1989) 340-347. [PMID: 2506427]

3. Moure, V.R., Costa, F.F., Cruz, L.M., Pedrosa, F.O., Souza, E.M., Li, X.D., Winkler, F. and Huergo, L.F. Regulation of nitrogenase by reversible mono-ADP-ribosylation. Curr. Top. Microbiol. Immunol. 384 (2015) 89-106. [PMID: 24934999]

[EC 2.4.2.37 created 1992, modified 2015]

EC 2.4.2.38

Accepted name: glycoprotein 2-β-D-xylosyltransferase

Reaction: UDP-D-xylose + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine = UDP + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-[β-D-xylosyl-(1→2)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine

For diagram click here.

Other name(s): β1,2-xylosyltransferase

Systematic name: UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase

Comments: Specific for N-linked oligosaccharides (N-glycans).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 141256-56-6

References:

1. Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340-31347. [PMID: 9395463]

2. Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105-108. [PMID: 10781814]

[EC 2.4.2.38 created 2001]

EC 2.4.2.39

Accepted name: xyloglucan 6-xylosyltransferase

Reaction: Transfers an α-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an α-(1→6)-D-xylosyl-D-glucose linkage

Other name(s): uridine diphosphoxylose-xyloglucan 6α-xylosyltransferase; xyloglucan 6-α-D-xylosyltransferase

Systematic name: UDP-D-xylose:xyloglucan 1,6-α-D-xylosyltransferase

Comments: In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80238-01-3

References:

1. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117-11122. [PMID: 6457048]

2. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells-synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517-523.

[EC 2.4.2.39 created 1989 as EC 2.4.1.169, transferred 2003 to EC 2.4.2.39]

EC 2.4.2.40

Accepted name: zeatin O-β-D-xylosyltransferase

Reaction: UDP-D-xylose + zeatin = UDP + O-β-D-xylosylzeatin

Glossary: zeatin

Other name(s): uridine diphosphoxylose-zeatin xylosyltransferase; zeatin O-xylosyltransferase

Systematic name: UDP-D-xylose:zeatin O-β-D-xylosyltransferase

Comments: Does not act on UDP-glucose (cf. EC 2.4.1.103 alizarin 2-β-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 110541-22-5

References:

1. Turner, J.E., Mok, D.W.S., Mok, M.C. and Shaw, G. Isolation and partial-purification of an enzyme catalyzing the formation of O-xylosylzeatin in Phaseolus vulgaris embryos. Proc. Natl. Acad. Sci. USA 84 (1987) 3714-3717.

[EC 2.4.2.40 created 1992 as EC 2.4.1.204, transferred 2003 to EC 2.4.2.40]

EC 2.4.2.41

Accepted name: xylogalacturonan β-1,3-xylosyltransferase

Reaction: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a β-1,3-D-xylosyl-D-galactose linkage.

Other name(s): xylogalacturonan xylosyltransferase; XGA xylosyltransferase

Systematic name: UDP-D-xylose:xylogalacturonan β-1,3-xylosyltransferase

Comments: Involved in plant cell wall synthesis. The enzyme from Arabidopsis thaliana also transfers D-xylose from UDP-D-xylose onto oligogalacturonide acceptors. The enzyme did not show significant activity with UDP-glucose, UDP-galactose, or UDP-N-acetyl-D-glucosamine as sugar donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jensen, J.K., Sorensen, S.O., Harholt, J., Geshi, N., Sakuragi, Y., Moller, I., Zandleven, J., Bernal, A.J., Jensen, N.B., Sorensen, C., Pauly, M., Beldman, G., Willats, W.G. and Scheller, H.V. Identification of a xylogalacturonan xylosyltransferase involved in pectin biosynthesis in Arabidopsis. Plant Cell 20 (2008) 1289-1302. [PMID: 18460606]

[EC 2.4.2.41 created 2009]

EC 2.4.2.42

Accepted name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase

Reaction: UDP-D-xylose + Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87) = UDP + Xylα(1-3)Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87)

Other name(s): β-glucoside α-1,3-xylosyltransferase

Systematic name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase

Comments: The enzyme is involved in the biosynthesis of the Xylα(1-3)Xylα(1-3)Glcβ-1-O-Ser on epidermal growth factor-like domains [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593-600. [PMID: 17317689]

2. Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143-146. [PMID: 9128735]

[EC 2.4.2.42 created 2010]

EC 2.4.2.43

Accepted name: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase

Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate

For diagram of reaction click here.

Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4'-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK, arnT (gene name)

Systematic name: 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase

Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122-43131. [PMID: 11535604]

2. Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132-43144. [PMID: 11535605]

3. Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111-43121. [PMID: 11535603]

4. Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33-39. [PMID: 16226890]

5. Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29-35. [PMID: 19947657]

[EC 2.4.2.43 created 2010, modified 2011]

EC 2.4.2.44

Accepted name: S-methyl-5'-thioinosine phosphorylase

Reaction: S-methyl-5'-thioinosine + phosphate = hypoxanthine + S-methyl-5-thio-α-D-ribose 1-phosphate

Other name(s): MTIP; MTI phosphorylase; methylthioinosine phosphorylase

Systematic name: S-methyl-5'-thioinosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase

Comments: No activity with S-methyl-5'-thioadenosine. The catabolism of of 5'-methylthioadenosine in Pseudomonas aeruginosa involves deamination to S-methyl-5'-thioinosine (EC 3.5.4.31, S-methyl-5'-thioadenosine deaminase) and phosphorolysis to hypoxanthine [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Guan, R., Ho, M.C., Almo, S.C. and Schramm, V.L. Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing. Biochemistry 50 (2011) 1247-1254. [PMID: 21197954]

[EC 2.4.2.44 created 2011]

EC 2.4.2.45

Accepted name: decaprenyl-phosphate phosphoribosyltransferase

Reaction: trans,octacis-decaprenyl phosphate + 5-phospho-α-D-ribose 1-diphosphate = trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate + diphosphate

For diagram of reaction click here.

Other name(s): 5-phospho-α-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase; 5-phospho-α-D-ribose 1-pyrophosphate:decaprenyl phosphate 5-phosphoribosyltransferase; DPPR synthase; Rv3806

Systematic name: trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate:diphosphate phospho-α-D-ribosyltransferase

Comments: Requires Mg2+. Isolated from Mycobacterium tuberculosis. Has some activity with other polyprenyl phosphates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Huang, H., Scherman, M.S., D'Haeze, W., Vereecke, D., Holsters, M., Crick, D.C. and McNeil, M.R. Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-α-D-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-D-arabinose synthesis. J. Biol. Chem. 280 (2005) 24539-24543. [PMID: 15878857]

[EC 2.4.2.45 created 2012]

EC 2.4.2.46

Accepted name: galactan 5-O-arabinofuranosyltransferase

Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→6)]14-β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol

For diagram of reaction click here.

Other name(s): AftA; Rv3792

Systematic name: galactofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 5-O-α-D-arabinofuranosyltransferase

Comments: Isolated from Mycobacterium tuberculosis and Corynebacterium glutamicum. These arabinofuranosyl groups form the start of an arabinofuranan chain as part of the of the cell wall in mycobacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Alderwick, L.J., Seidel, M., Sahm, H., Besra, G.S. and Eggeling, L. Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 281 (2006) 15653-15661. [PMID: 16595677]

[EC 2.4.2.46 created 2012]

EC 2.4.2.47

Accepted name: arabinofuranan 3-O-arabinosyltransferase

Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 3-O-position of an α-(1→5)-arabinofuranan chain attached to a β-(1→5)-galactofuranan chain

For diagram of reaction click here.

Other name(s): AftC

Systematic name: α-(1→5)-arabinofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 3-O-α-D-arabinofuranosyltransferase

Comments: Isolated from Mycobacterium smegmatis. Involved in the formation of the cell wall in mycobacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Birch, H.L., Alderwick, L.J., Bhatt, A., Rittmann, D., Krumbach, K., Singh, A., Bai, Y., Lowary, T.L., Eggeling, L. and Besra, G.S. Biosynthesis of mycobacterial arabinogalactan: identification of a novel α(1-→3) arabinofuranosyltransferase. Mol. Microbiol. 69 (2008) 1191-1206. [PMID: 18627460]

2. Zhang, J., Angala, S.K., Pramanik, P.K., Li, K., Crick, D.C., Liav, A., Jozwiak, A., Swiezewska, E., Jackson, M. and Chatterjee, D. Reconstitution of functional mycobacterial arabinosyltransferase AftC proteoliposome and assessment of decaprenylphosphorylarabinose analogues as arabinofuranosyl donors. ACS Chem. Biol. 6 (2011) 819-828. [PMID: 21595486]

[EC 2.4.2.47 created 2012]

EC 2.4.2.48

Accepted name: tRNA-guanine15 transglycosylase

Reaction: guanine15 in tRNA + 7-cyano-7-carbaguanine = 7-cyano-7-carbaguanine15 in tRNA + guanine

Glossary: 7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine
archaeosine = G* = 7-amidino-7-deazaguanosine

Other name(s): tRNA transglycosylase (ambiguous); transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine15 transglycosidase; TGT (ambiguous); transfer ribonucleic acid guanine15 transglycosylase

Systematic name: tRNA-guanine15:7-cyano-7-carbaguanine tRNA-D-ribosyltransferase

Comments: Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. This archaeal enzyme catalyses the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97) [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bai, Y., Fox, D.T., Lacy, J.A., Van Lanen, S.G. and Iwata-Reuyl, D. Hypermodification of tRNA in thermophilic archaea. Cloning, overexpression, and characterization of tRNA-guanine transglycosylase from Methanococcus jannaschii. J. Biol. Chem. 275 (2000) 28731-28738. [PMID: 10862614]

[EC 2.4.2.48 created 2012]

EC 2.4.2.49

Accepted name: neamine phosphoribosyltransferase

Reaction: neamine + 5-phospho-α-D-ribose 1-diphosphate = 5''-phosphoribostamycin + diphosphate

For diagram of reaction click here.

Glossary: neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol

Other name(s): btrL (gene name); neoM (gene name)

Systematic name: neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase

Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg2+, Ni2+ or Co2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360-4368. [PMID: 17482823]

[EC 2.4.2.49 created 2013]

EC 2.4.2.50

Accepted name: cyanidin 3-O-galactoside 2''-O-xylosyltransferase

Reaction: UDP-α-D-xylose + cyanidin 3-O-β-D-galactoside = UDP + cyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-galactoside)

For diagram of reaction click here.

Glossary: cyanidin = 3,3',4',5,7-pentahydroxyflavylium

Other name(s): CGXT

Systematic name: UDP-α-D-xylose:cyanidin-3-O-β-D-galactoside 2''-O-xylosyltransferase

Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397-403. [PMID: 8717136]

[EC 2.4.2.50 created 2013]

EC 2.4.2.51

Accepted name: anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase

Reaction: UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside

For diagram of reaction click here.

Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)

Other name(s): uridine 5'-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1

Systematic name: UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2'''-O-xylosyltransferase

Comments: Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Teusch, M. Uridine 5'-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559-563.

2. Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154-167. [PMID: 21899608]

[EC 2.4.2.51 created 2013]

EC 2.4.2.52

Accepted name: triphosphoribosyl-dephospho-CoA synthase

Reaction: ATP + 3'-dephospho-CoA = 2'-(5-triphospho-α-D-ribosyl)-3'-dephospho-CoA + adenine

For diagram of reaction click here.

Other name(s): 2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase; ATP:dephospho-CoA 5-triphosphoribosyl transferase; CitG; ATP:dephospho-CoA 5'-triphosphoribosyl transferase; MdcB; ATP:3-dephospho-CoA 5''-triphosphoribosyltransferase; MadG

Systematic name: ATP:3'-dephospho-CoA 5-triphosphoribosyltransferase

Comments: ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new α (1''→2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (γ-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 313345-38-9

References:

1. Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438-9450. [PMID: 10924139]

2. Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165-168. [PMID: 11042274]

3. Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439-2446. [PMID: 11948157]

4. Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223-13232. [PMID: 11052675]

[EC 2.4.2.52 created 2002 as EC 2.7.8.25, modified 2008, transferred 2013 to EC 2.4.2.52]

EC 2.4.2.53

Accepted name: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

Reaction: UDP-4-deoxy-4-formamido-β-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate

For diagram of reaction click here.

Other name(s): undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase; polymyxin resistance protein PmrF; UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,polycis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase

Systematic name: UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase

Comments: The enzyme shows no activity with UDP-4-amino-4-deoxy-β-L-arabinose.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number:

References:

1. Breazeale, S.D., Ribeiro, A.A. and Raetz, C.R. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277 (2002) 2886-2896. [PMID: 11706007]

2. Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154-14167. [PMID: 15695810]

[EC 2.4.2.53 created 2010 as EC 2.7.8.30, modified 2011, transferred 2013 to EC 2.4.2.53]

EC 2.4.2.54

Accepted name: β-ribofuranosylphenol 5'-phosphate synthase

Reaction: 5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate

For diagram of reaction click here.

Other name(s): β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5'-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect)

Systematic name: 5-phospho-α-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating)

Comments: The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It was initially thought to use 4-aminobenzoate as a substrate, but was later shown to utilize 4-hydroxybenzoate [4]. The activity is dependent on Mg2+ or Mn2+ [1].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343-11351. [PMID: 9698382]

2. Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442-4448. [PMID: 12142414]

3. Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389-39395. [PMID: 15262968]

4. White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041-6052. [PMID: 21634403]

[EC 2.4.2.54 created 2013, modified 2014, modified 2015]

EC 2.4.2.55

Accepted name: nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase

Reaction: nicotinate D-ribonucleotide + phenol = nicotinate + phenyl 5-phospho-α-D-ribofuranoside

Other name(s): ArsAB

Systematic name: nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase

Comments: The enzyme is involved in the biosynthesis of phenolic cobamides in the Gram-positive bacterium Sporomusa ovata. It can also transfer the phospho-D-ribosyl group to 4-methylphenol and 5,6-dimethylbenzimidazole. The related EC 2.4.2.21, nicotinate-nucleotide dimethylbenzimidazole phosphoribosyltransferase, also transfers the phospho-D-ribosyl group from nicotinate D-ribonucleotide to 5,6-dimethylbenzimidazole, but shows no activity with 4-methylphenol or phenol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Chan, C.H. and Escalante-Semerena, J.C. ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis. Mol. Microbiol. 81 (2011) 952-967. [PMID: 21696461]

[EC 2.4.2.55 created 2013]

EC 2.4.2.56

Accepted name: kaempferol 3-O-xylosyltransferase

Reaction: UDP-α-D-xylose + kaempferol = UDP + kaempferol 3-O-β-D-xyloside

For diagram of reaction, click here

Other name(s): F3XT; UDP-D-xylose:flavonol 3-O-xylosyltransferase; flavonol 3-O-xylosyltransferase

Systematic name: UDP-α-D-xylose:kaempferol 3-O-D-xylosyltransferase

Comments: The enzyme from the plant Euonymus alatus also catalyses the 3-O-D-xylosylation of other flavonols (e.g. quercetin, isorhamnetin, rhamnetin, myricetin, fisetin) with lower activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ishikura, N. and Yang, Z.Q. UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of Euonymus alatus f. ciliato-dentatus. Z. Naturforsch. C: Biosci. 46 (1991) 1003-1010.

[EC 2.4.2.56 created 2013]

EC 2.4.2.57

Accepted name: AMP phosphorylase

Reaction: (1) AMP + phosphate = adenine + α-D-ribose 1,5-bisphosphate
(2) CMP + phosphate = cytosine + α-D-ribose 1,5-bisphosphate
(3) UMP + phosphate = uracil + α-D-ribose 1,5-bisphosphate

For diagram of reaction click here.

Other name(s): AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name)

Systematic name: AMP:phosphate α-D-ribosyl 5'-phosphate-transferase

Comments: The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sato, T., Atomi, H. and Imanaka, T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003-1006. [PMID: 17303759]

2. Aono, R., Sato, T., Yano, A., Yoshida, S., Nishitani, Y., Miki, K., Imanaka, T. and Atomi, H. Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway. J. Bacteriol. 194 (2012) 6847-6855. [PMID: 23065974]

3. Nishitani, Y., Aono, R., Nakamura, A., Sato, T., Atomi, H., Imanaka, T. and Miki, K. Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization. J. Mol. Biol. (2013) . [PMID: 23659790]

[EC 2.4.2.57 created 2014]

EC 2.4.2.58

Accepted name: hydroxyproline O-arabinosyltransferase

Reaction: UDP-β-L-arabinofuranose + [protein]-trans-4-hydroxy-L-proline = UDP + [protein]-O-(β-L-arabinofuranosyl)-trans-4-hydroxy-L-proline

Glossary: trans-4-hydroxy-L-proline = (2S,4R)-4-hydroxyproline = (4R)-4-hydroxy-L-proline

Other name(s): HPAT

Systematic name: UDP-β-L-arabinofuranose:[protein]-trans-4-hydroxy-L-proline L-arabinofuranosyl transferase (configuration-retaining)

Comments: The enzyme, found in plants and mosses, catalyses the O-arabinosylation of hydroxyprolines in hydroxyproline-rich glycoproteins. The enzyme acts on the first hydroxyproline in the motif Val-hydroxyPro-hydroxyPro-Ser.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Ogawa-Ohnishi, M., Matsushita, W. and Matsubayashi, Y. Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana. Nat. Chem. Biol. 9 (2013) 726-730. [PMID: 24036508]

[EC 2.4.2.58 created 2016]


Continued with EC 2.4.99.1 to EC 2.4.99.11
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