Enzyme Nomenclature

Continued from EC 2.4.99

EC 2.5

Transferring Alkyl or Aryl Groups, Other than Methyl Groups

EC 2.5.1

See separate file for EC 2.5.1.51 to EC 2.5.1.100 and EC 2.5.1.101 to EC 2.5.1.141

Contents

EC 2.5.1.1 dimethylallyltranstransferase
EC 2.5.1.2 thiamine pyridinylase
EC 2.5.1.3 thiamine-phosphate diphosphorylase
EC 2.5.1.4 adenosylmethionine cyclotransferase
EC 2.5.1.5 galactose-6-sulfurylase
EC 2.5.1.6 methionine adenosyltransferase
EC 2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransferase
EC 2.5.1.8 transferred now EC 2.5.1.75
EC 2.5.1.9 riboflavin synthase
EC 2.5.1.10 (2E,6E)-farnesyl diphosphate synthase
EC 2.5.1.11 transferred now covered by EC 2.5.1.84 and EC 2.5.1.85
EC 2.5.1.12 deleted, included in EC 2.5.1.18
EC 2.5.1.13 deleted, included in EC 2.5.1.18
EC 2.5.1.14 deleted, included in EC 2.5.1.18
EC 2.5.1.15 dihydropteroate synthase
EC 2.5.1.16 spermidine synthase
EC 2.5.1.17 cob(I)yrinic acid a,c-diamide adenosyltransferase
EC 2.5.1.18 glutathione transferase
EC 2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase
EC 2.5.1.20 rubber cis-polyprenylcistransferase
EC 2.5.1.21 squalene synthase
EC 2.5.1.22 spermine synthase
EC 2.5.1.23 sym-norspermidine synthase
EC 2.5.1.24 discadenine synthase
EC 2.5.1.25 tRNA-uridine aminocarboxypropyltransferase
EC 2.5.1.26 alkylglycerone-phosphate synthase
EC 2.5.1.27 adenylate dimethylallyltransferase (AMP-dependent)
EC 2.5.1.28 dimethylallylcistransferase
EC 2.5.1.29 geranylgeranyl diphosphate synthase
EC 2.5.1.30 heptaprenyl diphosphate synthase
EC 2.5.1.31 ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific
EC 2.5.1.32 15-cis-phytoene synthase
EC 2.5.1.33 transferred now covered by EC 2.5.1.82 and EC 2.5.1.83
EC 2.5.1.34 4-dimethylallyltryptophan synthase
EC 2.5.1.35 aspulvinone dimethylallyltransferase
EC 2.5.1.36 trihydroxypterocarpan dimethylallyltransferase
EC 2.5.1.37 now EC 4.4.1.20
EC 2.5.1.38 isonocardicin synthase
EC 2.5.1.39 4-hydroxybenzoate polyprenyltransferase
EC 2.5.1.40 now EC 4.2.3.9
EC 2.5.1.41 phosphoglycerol geranylgeranyltransferase
EC 2.5.1.42 geranylgeranylglycerol-phosphate geranylgeranyltransferase
EC 2.5.1.43 nicotianamine synthase
EC 2.5.1.44 homospermidine synthase
EC 2.5.1.45 homospermidine synthase (spermidine-specific)
EC 2.5.1.46 deoxyhypusine synthase
EC 2.5.1.47 cysteine synthase
EC 2.5.1.48 cystathionine γ-synthase
EC 2.5.1.49 O-acetylhomoserine aminocarboxypropyltransferase
EC 2.5.1.50 zeatin 9-aminocarboxyethyltransferase

See the following files for:

EC 2.5.1.51 to EC 2.5.1.100
EC 2.5.1.101 to EC 2.5.1.141

Entries

EC 2.5.1.1

Accepted name: dimethylallyltranstransferase

Reaction: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate

For reaction pathway click here.

Other name(s): geranyl-diphosphate synthase; prenyltransferase; dimethylallyltransferase; DMAPP:IPP-dimethylallyltransferase; (2E,6E)-farnesyl diphosphate synthetase; diprenyltransferase; geranyl pyrophosphate synthase; geranyl pyrophosphate synthetase; trans-farnesyl pyrophosphate synthetase

Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallyltranstransferase

Comments: This enzyme will not accept larger prenyl diphosphates as efficient donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-79-5

References:

1. Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91-100.

2. Sagami, H., Ogura, K., Seto, S. and Kurokawa, T. A new prenyltransferase from Micrococcus lysodeikticus. Biochem. Biophys. Res. Commun. 85 (1978) 572-578. [PMID: 736921]

[EC 2.5.1.1 created 1961]

EC 2.5.1.2

Accepted name: thiamine pyridinylase

Reaction: thiamine + pyridine = 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole

For diagram click here.

Other name(s): pyrimidine transferase; thiaminase I; thiamin hydrolase; thiamin pyridinolase; thiaminase; thiamine pyridinolase; thiamin pyridinylase; thiamin:base 2-methyl-4-aminopyrimidine-5-methenyltransferase

Systematic name: thiamine:base 2-methyl-4-aminopyrimidine-5-methenyltransferase

Comments: Various bases and thiol compounds can act instead of pyridine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-35-7

References:

1. Fujita, A. Thiaminases. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 389-421.

2. Kenten, R.H. The partial purification and properties of a thiaminase from bracken [Pteridium aquilinum (L.) Kuhn]. Biochem. J. 67 (1957) 25-33.

3. Wittliff, J.L. and Airth, R.L. The extracellular thiaminase I of Bacillus thiaminolyticus. I. Purification and physicochemical properties. Biochemistry 7 (1968) 736-744. [PMID: 4966932]

[EC 2.5.1.2 created 1961, modified 1976, modified 2001]

EC 2.5.1.3

Accepted name: thiamine phosphate synthase

Reaction: (1) 4-amino-2-methyl-5-(diphosphomethyl)pyrimidine + 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate = diphosphate + thiamine phosphate + CO2
(2) 4-amino-2-methyl-5-(diphosphomethyl)pyrimidine + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO2
(3) 4-amino-2-methyl-5-(diphosphomethyl)pyrimidine + 4-methyl-5-(2-phosphonooxyethyl)thiazole = diphosphate + thiamine phosphate

For diagram of reaction click here.

Other name(s): thiamine phosphate pyrophosphorylase; thiamine monophosphate pyrophosphorylase; TMP-PPase; thiamine-phosphate diphosphorylase; thiE (gene name); TH1 (gene name); THI6 (gene name); 2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2-phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase

Systematic name: 4-amino-2-methyl-5-diphosphomethylpyrimidine:2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl-phosphate (4-amino-2-methylpyrimidin-5-yl)methyltransferase (decarboxylating)

Comments: The enzyme catalyses the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. The enzyme is thought to accept the product of EC 2.8.1.10, thiazole synthase, as its substrate. However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, thiazole tautomerase (EC 5.3.99.10) converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. In yeast this activity is found in a bifunctional enzyme (THI6) and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme (TH1).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-30-2

References:

1. Camiener, G.W. and Brown, G.M. The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates. J. Biol. Chem. 235 (1960) 2411-2417. [PMID: 13807175]

2. Leder, I.G. The enzymatic synthesis of thiamine monophosphate. J. Biol. Chem. 236 (1961) 3066-3071. [PMID: 14463407]

3. Kawasaki, Y. Copurification of hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase of Saccharomyces cerevisiae: characterization of hydroxyethylthiazole kinase as a bifunctional enzyme in the thiamine biosynthetic pathway. J. Bacteriol. 175 (1993) 5153-5158. [PMID: 8394314]

4. Backstrom, A.D., McMordie, R.A.S. and Begley, T.P. Biosynthesis of thiamin I: the function of the thiE gene product. J. Am. Chem. Soc. 117 (1995) 2351-2352.

5. Chiu, H.J., Reddick, J.J., Begley, T.P. and Ealick, S.E. Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 Å resolution. Biochemistry 38 (1999) 6460-6470. [PMID: 10350464]

6. Ajjawi, I., Tsegaye, Y. and Shintani, D. Determination of the genetic, molecular, and biochemical basis of the Arabidopsis thaliana thiamin auxotroph th1. Arch. Biochem. Biophys. 459 (2007) 107-114. [PMID: 17174261]

[EC 2.5.1.3 created 1965, modified 2015]

EC 2.5.1.4

Accepted name: adenosylmethionine cyclotransferase

Reaction: S-adenosyl-L-methionine = S-methyl-5'-thioadenosine + 2-aminobutan-4-olide

Other name(s): adenosylmethioninase

Systematic name: S-adenosyl-L-methionine alkyltransferase (cyclizing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-34-6

References:

1. Mudd, S.H. Enzymatic cleavage of S-adenosylmethionine. J. Biol. Chem. 234 (1959) 87-92. [PMID: 13610898]

2. Mudd, S.H. The mechanism of the enzymatic cleavage of S-adenosylmethionine to α-amino-γ-butyrolactone. J. Biol. Chem. 234 (1959) 1784-1786. [PMID: 13672964]

[EC 2.5.1.4 created 1965]

EC 2.5.1.5

Accepted name: galactose-6-sulfurylase

Reaction: Eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues

Glossary entries:
porphyran: a polysaccharide
Other name(s): porphyran sulfatase; galactose-6-sulfatase; galactose 6-sulfatase

Systematic name: D-galactose-6-sulfate:alkyltransferase (cyclizing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-36-8

References:

1. Rees, D.A. Enzymic desulphation of porphyran. Biochem. J. 80 (1961) 449-453.

2. Rees, D.A. Enzymic synthesis of 3:6-anhydro-L-galactose within porphyran from L-galactose 6-sulphate units. Biochem. J. 81 (1961) 347-352.

[EC 2.5.1.5 created 1965]

EC 2.5.1.6

Accepted name: methionine adenosyltransferase

Reaction: ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine

For diagram of reaction click here.

Other name(s): adenosylmethionine synthetase; ATP-methionine adenosyltransferase; methionine S-adenosyltransferase; methionine-activating enzyme; S-adenosyl-L-methionine synthetase; S-adenosylmethionine synthase; S-adenosylmethionine synthetase; AdoMet synthetase

Systematic name: ATP:L-methionine S-adenosyltransferase

Comments: Formerly EC 2.4.2.13, methionine adenosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-52-6

References:

1. Cantoni, G.L. S-Adenosylmethionine: A new intermediate formed enzymatically from L-methionine and adenosinetriphosphate. J. Biol. Chem. 204 (1953) 403-416.

2. Cantoni, G.L. and Durell, J. Activation of methionine for transmethylation. II. The methionine-activating enzyme: studies on the mechanism of reaction. J. Biol. Chem. 225 (1957) 1033-1048.

3. Mudd, S.H. and Cantoni, G.L. Activation of methionine for transmethylation. III. The methionine-activating enzyme of bakers' yeast. J. Biol. Chem. 231 (1958) 481-492.

[EC 2.5.1.6 created 1961 as EC 2.4.2.13, transferred 1965 to EC 2.5.1.6]

EC 2.5.1.7

Accepted name: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Reaction: phosphoenolpyruvate + UDP-N-acetyl-α-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine

For diagram click here.

Other name(s): MurA transferase; UDP-N-acetylglucosamine 1-carboxyvinyl-transferase; UDP-N-acetylglucosamine enoylpyruvyltransferase; enoylpyruvate transferase; phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase; phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase; phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase; phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose 3-enolpyruvyltransferase; phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase; pyruvate-UDP-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetyl-glucosamine transferase; pyruvic-uridine diphospho-N-acetylglucosaminyltransferase; phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase

Systematic name: phosphoenolpyruvate:UDP-N-acetyl-α-D-glucosamine 1-carboxyvinyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-27-2

References:

1. Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine. J. Biol. Chem. 243 (1968) 5770-5778. [PMID: 5699062]

2. Zemell, R.I. and Anwar, R.A. Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Purification to homogeneity and feedback inhibition. J. Biol. Chem. 250 (1975) 3185-3192. [PMID: 1123336]

3. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]

[EC 2.5.1.7 created 1972, modified 1983, modified 2002]

[EC 2.5.1.8 Transferred entry: tRNA isopentenyltransferase. As it is now known that the substrate is dimethyallyl diphosphate, the enzyme has been transferred to EC 2.5.1.75, tRNA dimethylallyltransferase. (EC 2.5.1.8 created 1972, deleted 2009)]

EC 2.5.1.9

Accepted name: riboflavin synthase

Reaction: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine

For diagram of reaction click here and mechanism (mechanism).

Other name(s): heavy riboflavin synthase; light riboflavin synthase; riboflavin synthetase; riboflavine synthase; riboflavine synthetase

Systematic name: 6,7-dimethyl-8-(1-D-ribityl)lumazine:6,7-dimethyl-8-(1-D-ribityl)lumazine 2,3-butanediyltransferase

Comments: A flavoprotein (riboflavin).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-82-5

References:

1. Plaut, G.W.E. Studies on the nature of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin. J. Biol. Chem. 238 (1963) 2225-2243.

2. Plaut, G.W.E. and Harvey, R.A. Riboflavin synthetase. Methods Enzymol. 18B (1971) 527-538.

3. Wacker, H., Harvey, R.A., Winestock, C.H. and Plaut, G.W.E. 4-(1'-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second product of the riboflavin synthetase reaction. J. Biol. Chem. 239 (1964) 3493-3497.

[EC 2.5.1.9 created 1972]

EC 2.5.1.10

Accepted name: (2E,6E)-farnesyl diphosphate synthase

Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate

For diagram of reaction, click here

Other name(s): farnesyl-diphosphate synthase; geranyl transferase I; prenyltransferase; farnesyl pyrophosphate synthetase; farnesylpyrophosphate synthetase; geranyltranstransferase

Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase

Comments: Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. The enzyme will not accept larger prenyl diphosphates as efficient donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37277-79-5

References:

1. Lynen, F., Agranoff, B.W., Eggerer, H., Henning, V. and Möslein, E.M. Zur Biosynthese der Terpene. VI. γ,γ-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat, biologische Vorstufen des Squalens. Angew. Chem. 71 (1959) 657-663.

2. Ogura, K., Nishino, T. and Seto, S. The purification of prenyltransferase and isopentenyl pyrophosphate isomerase of pumpkin fruit and their some properties. J. Biochem. (Tokyo) 64 (1968) 197-203. [PMID: 4303505]

3. Reed, B.C. and Rilling, H. Crystallization and partial characterization of prenyltransferase from avian liver. Biochemistry 14 (1975) 50-54. [PMID: 1109590]

4. Takahashi, I. and Ogura, K. Farnesyl pyrophosphate synthetase from Bacillus subtilis. J. Biochem. (Tokyo) 89 (1981) 1581-1587. [PMID: 6792191]

5. Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527-1537. [PMID: 6818223]

[EC 2.5.1.10 created 1972, modified 2010]

[EC 2.5.1.11 Transferred entry: trans-octaprenyltranstransferase. Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]) (EC 2.5.1.11 created 1972, deleted 2010)]

[EC 2.5.1.12 Deleted entry: glutathione S-alkyltransferase. Now included with EC 2.5.1.18 glutathione transferase (EC 2.5.1.12 created 1972, deleted 1976)]

[EC 2.5.1.13 Deleted entry: glutathione S-aryltransferase. Now included with EC 2.5.1.18 glutathione transferase (EC 2.5.1.13 created 1972, deleted 1976)]

[EC 2.5.1.14 Deleted entry: glutathione S-aralkyltransferase. Now included with EC 2.5.1.18 glutathione transferase (EC 2.5.1.14 created 1972, deleted 1976)]

EC 2.5.1.15

Accepted name: dihydropteroate synthase

Reaction: (7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + 7,8-dihydropteroate

For diagram of reaction click here.

Glossary: 7,8-dihydropteroate = 4-{[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino}benzoate

Other name(s): dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydropteroate synthetase; 7,8-dihydropteroic acid synthetase; dihydropteroate synthetase; dihydropteroic synthetase; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase; (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase

Systematic name: (7,8-dihydropterin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxy-7,8-dihydropteridine-6-methenyltransferase

Comments: The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase [4], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase [3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9055-61-2

References:

1. Richey, D.P. and Brown, G.M. The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J. Biol. Chem. 244 (1969) 1582-1592. [PMID: 4304228]

2. Shiota, T., Baugh, C.M., Jackson, R. and Dillard, R. The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate. Biochemistry 8 (1969) 5022-5028. [PMID: 4312465]

3. Güldener, U., Koehler, G.J., Haussmann, C., Bacher, A., Kricke, J., Becher, D. and Hegemann, J.H. Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth. Mol. Biol. Cell 15 (2004) 3811-3828. [PMID: 15169867]

4. Storozhenko, S., Navarrete, O., Ravanel, S., De Brouwer, V., Chaerle, P., Zhang, G.F., Bastien, O., Lambert, W., Rebeille, F. and Van Der Straeten, D. Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response. J. Biol. Chem. 282 (2007) 10749-10761. [PMID: 17289662]

[EC 2.5.1.15 created 1972, modified 2015]

EC 2.5.1.16

Accepted name: spermidine synthase

Reaction: S-adenosyl 3-(methylthio)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine

For diagram of reaction click here.

Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N'-bis(3-aminopropyl)butane-1,4-diamine
putrescine = butane-1,4-diamine
S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium

Other name(s): aminopropyltransferase; putrescine aminopropyltransferase; spermidine synthetase; SpeE; S-adenosylmethioninamine:putrescine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase

Comments: The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37277-82-0

References:

1. Hannonen, P., Janne, J. and Raina, A. Partial purification and characterization of spermine synthase from rat brain. Biochim. Biophys. Acta 289 (1972) 225-231. [PMID: 4564056]

2. Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315-320. [PMID: 6798961]

3. Tabor, C.W. Propylamine transferase (spermidine synthesis). Methods Enzymol. 5 (1962) 761-765.

4. Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 203-268. [PMID: 4628436]

5. Bowman, W.H., Tabor, C.W. and Tabor, H. Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J. Biol. Chem. 248 (1973) 2480-2486. [PMID: 4572733]

6. Korolev, S., Ikeguchi, Y., Skarina, T., Beasley, S., Arrowsmith, C., Edwards, A., Joachimiak, A., Pegg, A.E. and Savchenko, A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat. Struct. Biol. 9 (2002) 27-31. [PMID: 11731804]

7. Yoon, S.O., Lee, Y.S., Lee, S.H. and Cho, Y.D. Polyamine synthesis in plants: isolation and characterization of spermidine synthase from soybean (Glycine max) axes. Biochim. Biophys. Acta 1475 (2000) 17-26. [PMID: 10806333]

[EC 2.5.1.16 created 1972, modified 1982, modified 2013]

EC 2.5.1.17

Accepted name: cob(I)yrinic acid a,c-diamide adenosyltransferase

Reaction: (1) ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide

(2) ATP + cobinamide = triphosphate + adenosylcobinamide

For diagram click here.

Other name(s): CobA; CobO; ATP:corrinoid adenosyltransferase; cob(I)alamin adenosyltransferase; aquacob(I)alamin adenosyltransferase; aquocob(I)alamin vitamin B12s adenosyltransferase; ATP:cob(I)alamin Coβ-adenosyltransferase

Systematic name: ATP:cob(I)yrinic acid-a,c-diamide Coβ-adenosyltransferase

Comments: The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) to Co(II) by a one-electron transfer. This can be carried out by EC 1.16.1.3, aquacobalamin reductase or non-enzymically in the presence of dihydroflavin nucleotides [2]. (ii) Co(II) is reduced to Co(I) in a second single-electron transfer by EC 1.16.1.4, cob(II)alamin reductase and (iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP to leave the cobalt atom in a Co(III) state (EC 2.5.1.17). The enzyme responsible for the adenosylation reaction is the product of the gene cobO in the aerobic bacterium Pseudomonas denitrificans and of the gene cobA in the anaerobic bacterium Salmonella typhimurium. In P. denitrificans, the enzyme shows specificity for cobyrinic acid a,c-diamide and the corrinoids that occur later in the biosynthetic pathway whereas CobA seems to have broader specificity [3]. While CobA has a preference for ATP and Mn2+, it is able to transfer a variety of nucleosides to the cobalt, including CTP, UTP and GTP, in decreasing order of preference [4] and to use Mg2+ instead of Mn2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37277-84-2

References:

1. Vitols, E., Walker, G.A. and Huennekens, F.M. Enzymatic conversion of vitamin B12s to a cobamide coenzyme, α-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide (adenosyl-B12). J. Biol. Chem. 241 (1966) 1455-1461. [PMID: 5946606]

2. Bauer, C.B., Fonseca, M.V., Holden, H.M., Thoden, J.B., Thompson, T.B., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP. Biochemistry 40 (2001) 361-374. [PMID: 11148030]

3. Fonseca, M.V. and Escalante-Semerena, J.C. An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin. J. Biol. Chem. 276 (2001) 32101-32108. [PMID: 11408479]

4. Suh, S. and Escalante-Semerena, J.C. Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium. J. Bacteriol. 177 (1995) 921-925. [PMID: 7860601]

[EC 2.5.1.17 created 1972, modified 2004]

EC 2.5.1.18

Accepted name: glutathione transferase

Reaction: RX + glutathione = HX + R-S-glutathione

Other name(s): glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST

Systematic name: RX:glutathione R-transferase

Comments: A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 50812-37-8

References:

1. Habig, W.H., Pabst, M.J. and Jakoby, W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139. [PMID: 4436300]

2. Jakoby, W.B. The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 46 (1978) 383. [PMID: 345769]

3. Jakoby, W.B. Glutathione transferases: an overview. Methods Enzymol. 113 (1985) 495-499.

4. Keen, J.H. and Jakoby, W.B. Glutathione transferases. Catalysis of nucleophilic reactions of glutathione. J. Biol. Chem. 253 (1978) 5654-5657. [PMID: 670218]

5. Sheehan, D., Meade, G., Foley, V.M. and Dowd, C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16. [PMID: 11695986]

[EC 2.5.1.18 created 1976 (EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7 created 1972, incorporated 1976)]

EC 2.5.1.19

Accepted name: 3-phosphoshikimate 1-carboxyvinyltransferase

Reaction: phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate

For diagram click here and mechanism here.

Other name(s): 5-enolpyruvylshikimate-3-phosphate synthase; 3-enolpyruvylshikimate 5-phosphate synthase; 3-enolpyruvylshikimic acid-5-phosphate synthetase; 5'-enolpyruvylshikimate-3-phosphate synthase; 5-enolpyruvyl-3-phosphoshikimate synthase; 5-enolpyruvylshikimate-3-phosphate synthetase; 5-enolpyruvylshikimate-3-phosphoric acid synthase; enolpyruvylshikimate phosphate synthase; EPSP synthase

Systematic name: phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-73-9

References:

1. Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82-90. [PMID: 4289188]

[EC 2.5.1.19 created 1976, modified 1983, modified 1989]

EC 2.5.1.20

Accepted name: rubber cis-polyprenylcistransferase

Reaction: poly-cis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a poly-cis-polyprenyl diphosphate longer by one C5 unit

For diagram of reaction, click here.

Other name(s): rubber allyltransferase; rubber transferase; isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase; cis-prenyl transferase; rubber polymerase; rubber prenyltransferase

Systematic name: poly-cis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase

Comments: Rubber particles act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-41-6

References:

1. Archer, B.L. and Cockbain, E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476-480.

2. McMullen, A.I. and McSweeney, G.P. The biosynthesis of rubber. Incorporation of isopentenyl pyrophosphate into purified rubber particles by a soluble latex-serum enzyme. Biochem. J. 101 (1966) 42-47.

[EC 2.5.1.20 created 1976]

EC 2.5.1.21

Accepted name: squalene synthase

Reaction: 2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+ (overall reaction)
(1a) 2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
(1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+

For diagram of reaction click here

Other name(s): farnesyltransferase; presqualene-diphosphate synthase; presqualene synthase; squalene synthetase; farnesyl-diphosphate farnesyltransferase; SQS

Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase

Comments: This microsomal enzyme catalyses the first committed step in the biosynthesis of sterols. The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated. When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP) [8]. High concentrations of FPP inhibit the production of squalene but not of PSPP [8].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9077-14-9

References:

1. Kuswick-Rabiega, G. and Rilling, H.C. Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities. J. Biol. Chem. 262 (1987) 1505-1509. [PMID: 3805037]

2. Ericsson, J., Appelkvist, E.L., Thelin, A., Chojnacki, T. and Dallner, G. Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase. J. Biol. Chem. 267 (1992) 18708-18714. [PMID: 1527001]

3. Tansey, T.R. and Shechter, I. Structure and regulation of mammalian squalene synthase. Biochim. Biophys. Acta 1529 (2000) 49-62. [PMID: 11111077]

4. LoGrasso, P.V., Soltis, D.A. and Boettcher, B.R. Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase. Arch. Biochem. Biophys. 307 (1993) 193-199. [PMID: 8239656]

5. Shechter, I., Klinger, E., Rucker, M.L., Engstrom, R.G., Spirito, J.A., Islam, M.A., Boettcher, B.R. and Weinstein, D.B. Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase. J. Biol. Chem. 267 (1992) 8628-8635. [PMID: 1569107]

6. Agnew, W.S. and Popják, G. Squalene synthetase. Stoichiometry and kinetics of presqualene pyrophosphate and squalene synthesis by yeast microsomes. J. Biol. Chem. 253 (1978) 4566-4573. [PMID: 26684]

7. Pandit, J., Danley, D.E., Schulte, G.K., Mazzalupo, S., Pauly, T.A., Hayward, C.M., Hamanaka, E.S., Thompson, J.F. and Harwood, H.J., Jr. Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J. Biol. Chem. 275 (2000) 30610-30617. [PMID: 10896663]

8. Radisky, E.S. and Poulter, C.D. Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. Biochemistry 39 (2000) 1748-1760. [PMID: 10677224]

[EC 2.5.1.21 created 1976, modified 2005, modified 2012]

EC 2.5.1.22

Accepted name: spermine synthase

Reaction: S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine

For diagram of reaction click here.

Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N'-bis(3-aminopropyl)butane-1,4-diamine
S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium

Other name(s): spermidine aminopropyltransferase; spermine synthetase; S-adenosylmethioninamine:spermidine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase

Comments: The enzyme from mammalia is highly specific for spermidine [2,3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 74812-43-4

References:

1. Hibasami, H., Borchardt, R.T., Chen, S.-Y., Coward, J.K. and Pegg, A.E. Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem. J. 187 (1980) 419-428. [PMID: 7396856]

2. Pajula, R.-L., Raina, A. and Eloranta, T. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain. Eur. J. Biochem. 101 (1979) 619-626. [PMID: 520313]

3. Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315-320. [PMID: 6798961]

[EC 2.5.1.22 created 1982, modified 2013]

EC 2.5.1.23

Accepted name: sym-norspermidine synthase

Reaction: S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-thioadenosine + bis(3-aminopropyl)amine

Glossary: S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium

Other name(s): S-adenosylmethioninamine:propane-1,3-diamine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase

Comments: The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylthio)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).

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

References:

1. Aleksijevic, A., Grove, J. and Schuber, F. Studies on polyamine biosynthesis in Euglena gracilis. Biochim. Biophys. Acta 565 (1979) 199-207. [PMID: 116684]

2. Villanueva, V.R., Adlakha, R.C. and Calbayrac, R. Biosynthesis of polyamines in Euglena gracilis. Phytochemistry 19 (1980) 787-790.

3. Cacciapuoti, G., Porcelli, M., Carteni-Farina, M., Gambacorta, A. and Zappia, V. Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. Eur. J. Biochem. 161 (1986) 263-271. [PMID: 3096734]

[EC 2.5.1.23 created 1983, modified 2013]

EC 2.5.1.24

Accepted name: discadenine synthase

Reaction: S-adenosyl-L-methionine + N6-(Δ2-isopentenyl)-adenine = S-methyl-5'-thioadenosine + discadenine

Glossary: discadenine = 3-(3-amino-3-carboxypropyl)-N6-(Δ2-isopentenyl)-adenine

Other name(s): discadenine synthetase

Systematic name: S-adenosyl-L-methionine:N6-(Δ2-isopentenyl)-adenine 3-(3-amino-3-carboxypropyl)-transferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74082-52-3

References:

1. Taya, Y., Tanaka, Y. and Nishimura, S. Cell-free biosynthesis of discadenine, a spore germination inhibitor of Dictyostelium discoideum. FEBS Lett. 89 (1978) 326-328. [PMID: 566219]

[EC 2.5.1.24 created 1984]

EC 2.5.1.25

Accepted name: tRNA-uridine aminocarboxypropyltransferase

Reaction: S-adenosyl-L-methionine + uridine47 tRNAPhe = S-methyl-5'-thioadenosine + 3-[(3S)-3-amino-3-carboxypropyl]-uridine47 in tRNAPhe

Other name(s): S-adenosyl-L-methionine:tRNA-uridine 3-(3-amino-3-carboxypropyl)transferase

Systematic name: S-adenosyl-L-methionine:uridine47 in tRNAPhe 3-[(3S)-3-amino-3-carboxypropyl]transferase

Comments: The enzyme was studied in the bacterium Escherichia coli. The modification is found in the variable loop of the tRNA.

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

References:

1. Nishimura, S., Taya, Y., Kuchino, Y. and Ohashi, Z. Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia coli phenylalanine transfer RNA: transfer of the 3-amino-acid-3-carboxypropyl group from S-adenosylmethionine. Biochem. Biophys. Res. Commun. 57 (1974) 702-708. [PMID: 4597321]

[EC 2.5.1.25 created 1984, modified 2014]

EC 2.5.1.26

Accepted name: alkylglycerone-phosphate synthase

Reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion

Other name(s): alkyldihydroxyacetonephosphate synthase; alkyldihydroxyacetone phosphate synthetase; alkyl DHAP synthetase; alkyl-DHAP; dihydroxyacetone-phosphate acyltransferase; DHAP-AT

Systematic name: 1-acyl-glycerone-3-phosphate:long-chain-alcohol O-3-phospho-2-oxopropanyltransferase

Comments: The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 64060-42-0 and 102484-74-2

References:

1. Brown, A.J. and Snyder, F. Alkyldihydroxyacetone-P synthase. Solubilization, partial purification, new assay method, and evidence for a ping-pong mechanism. J. Biol. Chem. 257 (1982) 8835-8839. [PMID: 7096336]

2. Wykle, R.L., Piantadosi, C. and Snyder, F. The role of acyldihydroxyacetone phosphate, reduced nicotinamide adenine dinucleotide, and reduced nicotinamide adenine dinucleotide phosphate in the biosynthesis of O-alkyl glycerolipids by microsomal enzymes of Ehrlich ascites tumor. J. Biol. Chem. 247 (1972) 2944-2948. [PMID: 4401994]

[EC 2.5.1.26 created 1984]

EC 2.5.1.27

Accepted name: adenylate dimethylallyltransferase (AMP-dependent)

Reaction: dimethylallyl diphosphate + AMP = diphosphate + N6-(dimethylallyl)adenosine 5′-phosphate

For diagram of reaction, click here

Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:AMP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); IPT; adenylate dimethylallyltransferase

Systematic name: dimethylallyl-diphosphate:AMP dimethylallyltransferase

Comments: Involved in the biosynthesis of cytokinins in plants. Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112, adenylate dimethylallyltransferase (ADP/ATP-dependent).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72840-95-0

References:

1. Chen, C.-M. and Melitz, D.K. Cytokinin biosynthesis in a cell-free system from cytokinin-autotrophic tobacco tissue cultures. FEBS Lett. 107 (1979) 15-20. [PMID: 499537]

2. Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405-26410. [PMID: 11313355]

3. Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439-2446. [PMID: 15381407]

[EC 2.5.1.27 created 1984, modified 2002, modified 2013]

EC 2.5.1.28

Accepted name: dimethylallylcistransferase

Reaction: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate

For diagram of reaction, click here.

Other name(s): neryl-diphosphate synthase

Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase

Comments: This enzyme will not use larger prenyl diphosphates as efficient donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9032-79-5

References:

1. Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91-100.

2. Beytía, E., Valenzuela, P. and Cori, O. Terpene biosynthesis: formation of nerol, geraniol, and other prenols by an enzyme system from Pinus radiata seedlings. Arch. Biochem. Biophys. 129 (1969) 346-356.

[EC 2.5.1.28 created 1984]

EC 2.5.1.29

Accepted name: geranylgeranyl diphosphate synthase

Reaction: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate

For diagram of reaction click here

Other name(s): geranylgeranyl-diphosphate synthase; geranylgeranyl pyrophosphate synthetase; geranylgeranyl-PP synthetase; farnesyltransferase; geranylgeranyl pyrophosphate synthase; farnesyltranstransferase (obsolete)

Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase

Comments: Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-58-0

References:

1. Sagami, H., Ishi, K. and Ogura, K. Occurrence and unusual properties of geranylgeranyl pyrophosphate synthetase of pig liver. Biochem. Int. 3 (1981) 669-675.

[EC 2.5.1.29 created 1984, modified 2011]

EC 2.5.1.30

Accepted name: heptaprenyl diphosphate synthase

Reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate

For diagram of reaction, click here

Other name(s): all-trans-heptaprenyl-diphosphate synthase; heptaprenyl pyrophosphate synthase; heptaprenyl pyrophosphate synthetase; HepPP synthase; HepPS; heptaprenylpyrophosphate synthetase

Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units)

Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 74506-59-5

References:

1. Takahashi, I., Ogura, K. and Seto, S. Heptaprenyl pyrophosphate synthetase from Bacillus subtilis. J. Biol. Chem. 255 (1980) 4539-4543. [PMID: 6768722]

2. Zhang, Y.W., Koyama, T., Marecak, D.M., Prestwich, G.D., Maki, Y. and Ogura, K. Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex. Biochemistry 37 (1998) 13411-13420. [PMID: 9748348]

3. Zhang, Y.W., Li, X.Y., Sugawara, H. and Koyama, T. Site-directed mutagenesis of the conserved residues in component I of Bacillus subtilis heptaprenyl diphosphate synthase. Biochemistry 38 (1999) 14638-14643. [PMID: 10545188]

4. Suzuki, T., Zhang, Y.W., Koyama, T., Sasaki, D.Y. and Kurihara, K. Direct observation of substrate-enzyme complexation by surface forces measurement. J. Am. Chem. Soc. 128 (2006) 15209-15214. [PMID: 17117872]

[EC 2.5.1.30 created 1984, modified 2010]

EC 2.5.1.31

Accepted name: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]

Reaction: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate

For diagram of reaction click here

Other name(s): di-trans,poly-cis-undecaprenyl-diphosphate synthase; undecaprenyl-diphosphate synthase; bactoprenyl-diphosphate synthase; UPP synthetase; undecaprenyl diphosphate synthetase; undecaprenyl pyrophosphate synthetase; di-trans,poly-cis-decaprenylcistransferase

Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)

Comments: Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52350-87-5

References:

1. Muth, J.D. and Allen, C.M. Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein. Arch. Biochem. Biophys. 230 (1984) 49-60. [PMID: 6712246]

2. Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527-1537. [PMID: 6818223]

3. Guo, R.T., Ko, T.P., Chen, A.P., Kuo, C.J., Wang, A.H. and Liang, P.H. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J. Biol. Chem. 280 (2005) 20762-20774. [PMID: 15788389]

4. Ko, T.P., Chen, Y.K., Robinson, H., Tsai, P.C., Gao, Y.G., Chen, A.P., Wang, A.H. and Liang, P.H. Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 276 (2001) 47474-47482. [PMID: 11581264]

5. Fujikura, K., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. Biochemistry 42 (2003) 4035-4041. [PMID: 12680756]

6. Fujihashi, M., Zhang, Y.W., Higuchi, Y., Li, X.Y., Koyama, T. and Miki, K. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA 98 (2001) 4337-4342. [PMID: 11287651]

7. Pan, J.J., Chiou, S.T. and Liang, P.H. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Biochemistry 39 (2000) 10936-10942. [PMID: 10978182]

8. Kharel, Y., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. J. Biochem. 134 (2003) 819-826. [PMID: 14769870]

[EC 2.5.1.31 created 1984, modified 2011]

EC 2.5.1.32

Accepted name: 15-cis-phytoene synthase

Reaction: 2 geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate (overall reaction)
(1a) 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
(1b) prephytoene diphosphate = 15-cis-phytoene + diphosphate

For diagram of reaction click here

Other name(s): prephytoene-diphosphate synthase (ambiguous); phytoene synthetase (ambiguous); PSase (ambiguous); geranylgeranyl-diphosphate geranylgeranyltransferase (ambiguous)

Systematic name: geranylgeranyl-diphosphate:geranylgeranyl-diphosphate geranylgeranyltransferase (15-cis-phytoene forming)

Comments: Requires Mn2+ for activity. The enzyme produces 15-cis-phytoene. cf. EC 2.5.1.99, 15-trans-phytoene synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 50936-61-3

References:

1. Gregonis, D.E. and Rilling, H.C. The stereochemistry of trans-phytoene synthesis. Some observations on lycopersene as a carotene precursor and a mechanism for the synthesis of cis- and trans-phytoene. Biochemistry 13 (1974) 1538-1542. [PMID: 4819767]

2. Misawa, N., Truesdale, M.R., Sandmann, G., Fraser, P.D., Bird, C., Schuch, W. and Bramley, P.M. Expression of a tomato cDNA coding for phytoene synthase in Escherichia coli, phytoene formation in vivo and in vitro, and functional analysis of the various truncated gene products. J. Biochem. (Tokyo) 116 (1994) 980-985. [PMID: 7896759]

[EC 2.5.1.32 created 1984, modified 2005, modified 2012]

[EC 2.5.1.33 Transferred entry: trans-pentaprenyltranstransferase. Now covered by EC 2.5.1.82 (hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]) and EC 2.5.1.83 (hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]) (EC 2.5.1.33 created 1984, deleted 2010)]

EC 2.5.1.34

Accepted name: 4-dimethylallyltryptophan synthase

Reaction: dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan

For diagram of reaction click here.

Other name(s): dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase; dimethylallyltryptophan synthetase; dimethylallylpyrophosphate:tryptophan dimethylallyl transferase; DMAT synthetase; 4-(γ,γ-dimethylallyl)tryptophan synthase; tryptophan dimethylallyltransferase

Systematic name: dimethylallyl-diphosphate:L-tryptophan 4-dimethylallyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 55127-01-0

References:

1. Lee, S.L., Floss, H.G. and Heinstein, P. Purification and properties of dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps sp. SD 58. Arch. Biochem. Biophys. 177 (1976) 84-94. [PMID: 999297]

[EC 2.5.1.34 created 1984, modified 2010]

EC 2.5.1.35

Accepted name: aspulvinone dimethylallyltransferase

Reaction: 2 dimethylallyl diphosphate + aspulvinone E = 2 diphosphate + aspulvinone H

Other name(s): dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase

Systematic name: dimethylallyl-diphosphate:aspulvinone-E dimethylallyltransferase

Comments: This enzyme will also use as acceptor aspulvinone G, a hydroxylated derivative of the complex phenolic pigment aspulvinone E.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 67584-68-3

References:

1. Takahashi, I., Ojima, N., Ogura, K. and Seto, S. Purification and characterization of dimethylallyl pyrophosphate: aspulvinone dimethylallyltransferase from Aspergillus terreus. Biochemistry 17 (1978) 2696-2702. [PMID: 678538]

[EC 2.5.1.35 created 1984]

EC 2.5.1.36

Accepted name: trihydroxypterocarpan dimethylallyltransferase

Reaction: (1) dimethylallyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan

or

(2) dimethylallyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan

For diagram click here.

Other name(s): glyceollin synthase; dimethylallylpyrophosphate:3,6a,9-trihydroxypterocarpan dimethylallyltransferase; dimethylallylpyrophosphate:trihydroxypterocarpan dimethylallyl transferase; dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethyltransferase

Systematic name: dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethylallyltransferase

Comments: Part of the glyceollin biosynthesis system in soy bean.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70851-94-4

References:

1. Leube, J. and Grisebach, H. Further studies on induction of enzymes of phytoalexin synthesis in soybean and cultured soybean cells. Z. Naturforsch. C: Biosci. 38 (1983) 730-735.

2. Zähringer, U., Schaller, E. and Grisebach, H. Induction of phytoalexin synthesis in soybean. Structure and reactions of naturally occurring and enzymatically prepared prenylated pterocarpans from elicitor-treated cotyledons and cell cultures of soybean. Z. Natursforsch. C: Biosci. 36 (1981) 234-241.

[EC 2.5.1.36 created 1989]

[EC 2.5.1.37 Transferred entry: now EC 4.4.1.20, leukotriene-C4 synthase. The enzyme was incorrectly classified as a transferase. (EC 2.5.1.37 created 1989, deleted 2004)]

EC 2.5.1.38

Accepted name: isonocardicin synthase

Reaction: S-adenosyl-L-methionine + nocardicin G = S-methyl-5'-thioadenosine + isonocardicin C

For diagram of reaction click here Other name(s): nocardicin aminocarboxypropyltransferase; S-adenosyl-L-methionine:nocardicin-E 3-amino-3-carboxypropyltransferase

Systematic name: S-adenosyl-L-methionine:nocardicin-G 3-amino-3-carboxypropyltransferase

Comments: The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the β-lactam antibiotic nocardicin A. The enzyme can act on nocardicin E, F, and G, producing isonocardicin A, B, and C, respectively. However, the in vivo substrate is believed to be nocardicin G [3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118246-74-5

References:

1. Wilson, B.A., Bantia, S., Salituro, G.M., Reeve, A.M. and Townsend, C.A. Cell-free biosynthesis of nocardicin A from nocardicin E and S-adenosylmethionine. J. Am. Chem. Soc. 110 (1988) 8238-8239.

2. Reeve, A.M., Breazeale, S.D. and Townsend, C.A. Purification, characterization, and cloning of an S-adenosylmethionine-dependent 3-amino-3-carboxypropyltransferase in nocardicin biosynthesis. J. Biol. Chem. 273 (1998) 30695-30703. [PMID: 9804844]

3. Kelly, W.L. and Townsend, C.A. Mutational analysis of nocK and nocL in the nocardicin a producer Nocardia uniformis. J. Bacteriol. 187 (2005) 739-746. [PMID: 15629944]

[EC 2.5.1.38 created 1992, modified 2016]

EC 2.5.1.39

Accepted name: 4-hydroxybenzoate polyprenyltransferase

Reaction: a polyprenyl diphosphate + 4-hydroxybenzoate = diphosphate + a 4-hydroxy-3-polyprenylbenzoate

For diagram of reaction click here.

Other name(s): nonaprenyl-4-hydroxybenzoate transferase; 4-hydroxybenzoate transferase; p-hydroxybenzoate dimethylallyltransferase; p-hydroxybenzoate polyprenyltransferase; p-hydroxybenzoic acid-polyprenyl transferase; p-hydroxybenzoic-polyprenyl transferase; 4-hydroxybenzoate nonaprenyltransferase

Systematic name: polyprenyl-diphosphate:4-hydroxybenzoate polyprenyltransferase

Comments: This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound. The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency [2,4,5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-77-7

References:

1. Kalén, A., Appelkvist, E.-L., Chojnacki, T. and Dallner, G. Nonaprenyl-4-hydroxybenzoate transferase, an enzyme involved in ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system of rat liver. J. Biol. Chem. 265 (1990) 1158-1164. [PMID: 2295606]

2. Melzer, M. and Heide, L. Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim. Biophys. Acta 1212 (1994) 93-102. [PMID: 8155731]

3. Okada, K., Ohara, K., Yazaki, K., Nozaki, K., Uchida, N., Kawamukai, M., Nojiri, H. and Yamane, H. The AtPPT1 gene encoding 4-hydroxybenzoate polyprenyl diphosphate transferase in ubiquinone biosynthesis is required for embryo development in Arabidopsis thaliana. Plant Mol. Biol. 55 (2004) 567-577. [PMID: 15604701]

4. Forsgren, M., Attersand, A., Lake, S., Grunler, J., Swiezewska, E., Dallner, G. and Climent, I. Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ. Biochem. J. 382 (2004) 519-526. [PMID: 15153069]

5. Tran, U.C. and Clarke, C.F. Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion 7 Suppl (2007) S62-S71. [PMID: 17482885]

[EC 2.5.1.39 created 1992, modified 2010]

[EC 2.5.1.40 Transferred entry: now EC 4.2.3.9 aristolochene synthase (EC 2.5.1.40 created 1992, deleted 1999)]

EC 2.5.1.41

Accepted name: phosphoglycerol geranylgeranyltransferase

Reaction: geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate

For diagram of reaction click here.

Glossary: sn-glyceryl phosphate = sn-glycerol 1-phosphate = (S)-2,3-dihydroxypropyl dihydrogen phosphate

Other name(s): glycerol phosphate geranylgeranyltransferase; geranylgeranyl-transferase (ambiguous); prenyltransferase (ambiguous); (S)-3-O-geranylgeranylglyceryl phosphate synthase; (S)-geranylgeranylglyceryl phosphate synthase; GGGP synthase; (S)-GGGP synthase; GGGPS; geranylgeranyl diphosphate:sn-glyceryl phosphate geranylgeranyltransferase; geranylgeranyl diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase

Systematic name: geranylgeranyl-diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase

Comments: This cytosolic enzyme catalyses the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria [2]. Requires Mg2+ for maximal activity [2]. It catalyses the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase) and EC 2.7.7.67 (CDP-archaeol synthase), which lead to the formation of CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 124650-69-7

References:

1. Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264-1265.

2. Chen, A., Zhang, D. and Poulter, C.D. (S)-Geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis. J. Biol. Chem. 268 (1993) 21701-21705. [PMID: 8408023]

3. Nemoto, N., Oshima, T. and Yamagishi, A. Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum. J. Biochem. 133 (2003) 651-657. [PMID: 12801917]

4. Payandeh, J., Fujihashi, M., Gillon, W. and Pai, E.F. The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme. J. Biol. Chem. 281 (2006) 6070-6078. [PMID: 16377641]

5. Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568-36574. [PMID: 10960477]

[EC 2.5.1.41 created 1992, modified 2009]

EC 2.5.1.42

Accepted name: geranylgeranylglycerol-phosphate geranylgeranyltransferase

Reaction: geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate

For diagram of reaction click here.

Other name(s): geranylgeranyloxyglycerol phosphate geranylgeranyltransferase; geranylgeranyltransferase II; (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; DGGGP synthase; DGGGPS

Systematic name: geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase

Comments: This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity [2]. 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and α-glycerophosphate cannot act as prenyl-acceptor substrates [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [3]. Belongs in the UbiA prenyltransferase family [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124650-68-6

References:

1. Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264-1265.

2. Hemmi, H., Shibuya, K., Takahashi, Y., Nakayama, T. and Nishino, T. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J. Biol. Chem. 279 (2004) 50197-50203. [PMID: 15356000]

3. Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568-36574. [PMID: 10960477]

[EC 2.5.1.42 created 1992, modified 2009]

EC 2.5.1.43

Accepted name: nicotianamine synthase

Reaction: 3 S-adenosyl-L-methionine = 3 S-methyl-5'-thioadenosine + nicotianamine

For reaction pathway click here.

Systematic name: S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-L-methionine 3-amino-3-carboxypropyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 161515-44-2

References:

1. Higuchi, K., Kanazawa, K., Nishizawa, N.-K., Chino, M., Mori, S. Purification and characterization of nicotianamine synthase from Fe-deficient barley root. Plant Soil 165 (1994) 173-179.

[EC 2.5.1.43 created 1999]

EC 2.5.1.44

Accepted name: homospermidine synthase

Reaction: (1) 2 putrescine = sym-homospermidine + NH3 + H+
(2) putrescine + spermidine = sym-homospermidine + propane-1,3-diamine

For reaction pathway click here.

Glossary
dehydroputrescine = 4-iminobutan-1-amine
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine

Systematic name: putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)

Comments: The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: NAD+-dependent dehydrogenation of putrescine (1a), transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine (1b) and reduction of the imine intermediate to form homospermidine (1c). Hence the overall reaction is transfer of a 4-aminobutyl group. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group. The reaction of this enzyme occurs in three steps: (i) NAD+-dependent dehydrogenation of putrescine, (ii) transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine, (iii) reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. In the presence of putrescine, spermidine can function as a donor of the aminobutyl group, in which case, propane-1,3-diamine is released instead of ammonia. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 76106-84-8

References:

1. Tait, G.H. The formation of homospermidine by an enzyme from Rhodopseudomonas viridis. Biochem. Soc. Trans. 7 (1979) 199-200. [PMID: 437275]

2. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85. [PMID: 16526057]

3. Yamamoto, S., Nagata, S. and Kusaba, K. Purification and characterization of homospermidine synthase in Acinetobacter tartarogens ATCC 31105. J. Biochem. 114 (1993) 45-49. [PMID: 8407874]

4. Srivenugopal, K.S. and Adiga, P.R. Enzymatic synthesis of sym-homospermidine in Lathyrus sativus T (grass pea) seedlings. Biochem. J. 190 (1980) 461-464. [PMID: 7470060]

5. Ober, D., Tholl, D., Martin, W. and Hartmann, T. Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli. J. Gen. Appl. Microbiol. 42 (1996) 411-419.

6. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [PMID: 10611289]

[EC 2.5.1.44 created 1999, modified 2001]

EC 2.5.1.45

Accepted name: homospermidine synthase (spermidine-specific)

Reaction: spermidine + putrescine = sym-homospermidine + propane-1,3-diamine

For reaction pathway click here.

Glossary
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine
spermidine: N-(3-aminopropyl)butane-1,4-diamine

Systematic name: spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming)

Comments: The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (a) NAD+-dependent dehydrogenation of spermidine, (b) transfer of the 4-aminobutylidene group from dehydrospermidine to putrescine and (c) reduction of the imine intermediate to form homospermidine. This enzyme is more specific than EC 2.5.1.44, homospermidine synthase, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio).

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

References:

1. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85. [PMID: 16526057]

2. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [PMID: 10611289]

3. Ober, D., Harms, R. and Hartmann, T. Cloning and expression of homospermidine synthase from Senecio vulgaris: a revision. Phytochemistry 55 (2000) 311-316.

[EC 2.5.1.45 created 2001]

EC 2.5.1.46

Accepted name: deoxyhypusine synthase

Reaction: [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction)
(1a) spermidine + NAD+ = dehydrospermidine + NADH
(1b) dehydrospermidine + [enzyme]-lysine = N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine
(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine = N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine
(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ = [eIF5A-precursor]-deoxyhypusine + NAD+

For reaction pathway click here.

Glossary
deoxyhypusine: N6-(4-aminobutyl)lysine
hypusine: N6-(4-amino-2-hydroxybutyl)lysine
spermidine: N-(3-aminopropyl)butane-1,4-diamine

Systematic name: [eIF5A-precursor]-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming)

Comments: The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 127069-31-2

References:

1. Wolff, E.C., Park, M.H. and Folk, J.E. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+. J. Biol. Chem. 265 (1990) 4793-4799. [PMID: 1690726]

2. Wolff, E.C., Folk, J.E. and Park, M.H. Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase. J. Biol. Chem. 272 (1997) 15865-15871. [PMID: 9188485]

3. Chen, K.Y. and Liu, A.Y.C. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6 (1997) 105-109. [PMID: 9285092]

4. Ober, D. and Hartmann, T. Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity. J. Biol. Chem. 274 (1999) 32040-32047. [PMID: 10542236]

5. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved form deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [PMID: 10611289]

6. Wolff, E.C. and Park, M.H. Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation. Yeast 15 (1999) 43-50. [PMID: 10028184]

7. Wolff, E.C., Wolff. J. and Park, M.H. Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism. J. Biol. Chem. 275 (2000) 9170-9177. [PMID: 10734052]

8. Joe, Y.A., Wolff, E.C. and Park, M.H. Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins. J. Biol. Chem. 270 (1995) 22386-22392. [PMID: 7673224]

9. Tao, Y. and Chen, K.Y. Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA. J. Biol. Chem. 270 (1995) 23984-23987. [PMID: 7592594]

[EC 2.5.1.46 provisional version created 1999 as EC 1.1.1.249 deleted 1999, revised and reinstated 2001 as EC 2.5.1.46]

EC 2.5.1.47

Accepted name: cysteine synthase

Reaction: O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate

For diagram of reaction click here.

Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid

Other name(s): O-acetyl-L-serine sulfhydrylase; O-acetyl-L-serine sulfohydrolase; O-acetylserine (thiol)-lyase; O-acetylserine (thiol)-lyase A; O-acetylserine sulfhydrylase; O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide); acetylserine sulfhydrylase; cysteine synthetase; S-sulfocysteine synthase

Systematic name: O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase

Comments: A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (β-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-89-4

References:

1. Becker, M.A., Kredich, N.M. and Tomkins, G.M. The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2418-2427. [PMID: 4891157]

2. Hara, S., Payne, M.A., Schnackerz, K.D. and Cook, P.F. A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium. Protein Expr. Purif. 1 (1990) 70-76. [PMID 2152186]

3. Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum. Phytochemistry 26 (1987) 2699-2704.

4. Murakoshi, I., Kaneko, M., Koide, C. and Ikegami, F. Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by cysteine synthase. Phytochemistry 25 (1986) 2759-2763.

5. Tai, C.H., Burkhard, P., Gani, D., Jenn, T., Johnson, C. and Cook, P.F. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry 40 (2001) 7446-7452. [PMID: 11412097]

6. Bettati, S., Benci, S., Campanini, B., Raboni, S., Chirico, G., Beretta, S., Schnackerz, K.D., Hazlett, T.L., Gratton, E. and Mozzarelli, A. Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase. J. Biol. Chem. 275 (2000) 40244-40251. [PMID: 10995767]

[EC 2.5.1.47 created 1972 as 4.2.99.8, modified 1976, modified 1990, transferred 2002 to EC 2.5.1.47]

EC 2.5.1.48

Accepted name: cystathionine γ-synthase

Reaction: O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate

For diagram of reaction click here.

Other name(s): O-succinyl-L-homoserine succinate-lyase (adding cysteine); O-succinylhomoserine (thiol)-lyase; homoserine O-transsuccinylase; O-succinylhomoserine synthase; O-succinylhomoserine synthetase; cystathionine synthase; cystathionine synthetase; homoserine transsuccinylase

Systematic name: O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase

Comments: A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse β,γ-elimination to form 2-oxobutanoate, succinate and ammonia.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-70-0

References:

1. Flavin, M. and Slaughter, C. Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine. Biochim. Biophys. Acta 132 (1967) 400-405. [PMID: 5340123]

2. Kaplan, M.M. and Flavin, M. Cystathionine γ-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis. J. Biol. Chem. 241 (1966) 4463-4471. [PMID: 5922970]

3. Wiebers, J.L. and Garner, H.R. Homocysteine and cysteine synthetases of Neurospora crassa. Purification, properties, and feedback control of activity. J. Biol. Chem. 242 (1967) 12-23. [PMID: 6016326]

4. Wiebers, J.L. and Garner, H.R. Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli. J. Biol. Chem. 242 (1967) 5644-5649.

5. Clausen, T., Huber, R., Prade, L., Wahl, M.C. and Messerschmidt, A. Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5 Å resolution. EMBO J. 17 (1998) 6827-6838. [PMID: 9843488]

6. Ravanel, S., Gakiere, B., Job, D. and Douce, R. Cystathionine γ-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli. Biochem. J. 331 (1998) 639-648. [PMID: 9531508]

[EC 2.5.1.48 created 1972 as EC 4.2.99.9, transferred 2002 to EC 2.5.1.48]

EC 2.5.1.49

Accepted name: O-acetylhomoserine aminocarboxypropyltransferase

Reaction: O-acetyl-L-homoserine + methanethiol = L-methionine + acetate

For diagram click here.

Other name(s): O-acetyl-L-homoserine acetate-lyase (adding methanethiol); O-acetyl-L-homoserine sulfhydrolase; O-acetylhomoserine (thiol)-lyase; O-acetylhomoserine sulfhydrolase; methionine synthase (misleading)

Systematic name: O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase

Comments: Also reacts with other thiols and H2S, producing homocysteine or thioethers. The name methionine synthase is more commonly applied to EC 2.1.1.13, methionine synthase. The enzyme from baker's yeast also catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-90-7

References:

1. Kerr, D. O-Acetylhomoserine sulfhydrylase (Neurospora). Methods Enzymol. 17B (1971) 446-450.

2. Smith, I.K. and Thompson, J.F. Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies. Biochim. Biophys. Acta 184 (1969) 130-138. [PMID: 5791104]

3. Yamagata, S. and Takeshima, K. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme. J. Biochem. (Tokyo) 80 (1976) 777-785. [PMID: 795806]

4. Yamagata, S. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure. J. Biochem. (Tokyo) 80 (1976) 787-797. [PMID: 795807]

5. Yamagata, S., Takeshima, K. and Naikai, N. Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast. J. Biochem. (Tokyo) 75 (1974) 1221-1229. [PMID: 4609980]

6. Yamagata, S. Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms. Biochimie 71 (1989) 1125-1143. [PMID: 2517474]

7. Shimizu, H., Yamagata, S., Masui, R., Inoue, Y., Shibata, T., Yokoyama, S., Kuramitsu, S. and Iwama, T. Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product. Biochim. Biophys. Acta 1549 (2001) 61-72. [PMID: 11566369]

[EC 2.5.1.49 created 1972 as EC 4.2.99.10, transferred 2002 to EC 2.5.1.49]

EC 2.5.1.50

Accepted name: zeatin 9-aminocarboxyethyltransferase

Reaction: O-acetyl-L-serine + zeatin = lupinate + acetate

For diagram click here.

Glossary:
lupinic acid
zeatin
O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid

Other name(s): β-(9-cytokinin)-alanine synthase; β-(9-cytokinin)alanine synthase; O-acetyl-L-serine acetate-lyase (adding N6-substituted adenine); lupinate synthetase; lupinic acid synthase; lupinic acid synthetase

Systematic name: O-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase

Comments: The enzyme acts not only on zeatin but also on other N6-substituted adenines. The reaction destroys their cytokinin activity and forms the corresponding 3-(adenin-9-yl)-L-alanine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 88086-35-5

References:

1. Entsch, B., Parker, C.W. and Letham, D.S. An enzyme from lupin seeds forming alanine derivatives of cytokinins. Phytochemistry 22 (1983) 375-381.

2. Mok, D.W.S. and Mok, M.C. Cytokinin metabolism and action. Ann. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 89-118.

[EC 2.5.1.50 created 1984 as EC 4.2.99.13, transferred 2002 to EC 2.5.1.50]


Continued with EC 2.5.1.51 to EC 2.5.1.100
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