Enzyme Nomenclature

Continued from EC 2.7.8 and EC 2.7.9

EC 2.8 Transferring Sulfur-Containing Groups

EC 2.8.1 and EC 2.8.2

Sections

EC 2.8.1 Sulfurtransferases
EC 2.8.2 Sulfotransferases
EC 2.8.3 CoA-transferases

EC 2.8.4 Transferring alkylthio groups


EC 2.8.1 Sulfurtransferases

Contents

EC 2.8.1.1 thiosulfate sulfurtransferase
EC 2.8.1.2 3-mercaptopyruvate sulfurtransferase
EC 2.8.1.3 thiosulfate—thiol sulfurtransferase
EC 2.8.1.4 tRNA uracil 4-sulfurtransferase
EC 2.8.1.5 thiosulfate—dithiol sulfurtransferase
EC 2.8.1.6 biotin synthase
EC 2.8.1.7 cysteine desulfurase
EC 2.8.1.8 lipoyl synthase
EC 2.8.1.9 molybdenum cofactor sulfurtransferase
EC 2.8.1.10 thiazole synthase
EC 2.8.1.11 molybdopterin synthase sulfurtransferase
EC 2.8.1.12 molybdopterin synthase
EC 2.8.1.13 tRNA-uridine 2-sulfurtransferase
EC 2.8.1.14 tRNA-5-taurinomethyluridine 2-sulfurtransferase
EC 2.8.1.15 tRNA-5-methyluridine54 2-sulfurtransferase


Entries

EC 2.8.1.1

Accepted name: thiosulfate sulfurtransferase

Reaction: thiosulfate + cyanide = sulfite + thiocyanate

Other name(s): thiosulfate cyanide transsulfurase; thiosulfate thiotransferase; rhodanese; rhodanase

Systematic name: thiosulfate:cyanide sulfurtransferase

Comments: A few other sulfur compounds can act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-04-4

References:

1. Sörbo, B.H. Crystalline rhodanese. I. Purification and physicochemical examination. Acta Chem. Scand. 7 (1953) 1129-1136.

2. Sörbo, B.H. Crystalline rhodanese. II. The enzyme catalyzed reaction. Acta Chem. Scand. 7 (1953) 1137-1145.

3. Westley, J. and Green, J.R. Crystalline beef kidney rhodanese. J. Biol. Chem. 234 (1959) 2325-2326.

[EC 2.8.1.1 created 1961]

EC 2.8.1.2

Accepted name: 3-mercaptopyruvate sulfurtransferase

Reaction: 3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

Other names: β-mercaptopyruvate sulfurtransferase

Systematic name: 3-mercaptopyruvate:cyanide sulfurtransferase

Comments: Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. The bacterial enzyme is a zinc protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-05-5

References:

1. Fiedler, H. and Wood, J.L. Specificity studies on the β-mercaptopyruvate-cyanide transsulfuration system. J. Biol. Chem. 222 (1956) 387-397.

2. Hylin, J.W. and Wood, J.L. Enzymatic formation of polysulfides from mercaptopyruvate. J. Biol. Chem. 234 (1959) 2141-2144.

3. Sörbo, B.H. Enzymic transfer of sulfur from mercaptopyruvate to sulfite or sulfinates. Biochem. Biophys. Acta 24 (1957) 324-329.

4. Vachek, H. and Wood, J.L. Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli. Biochim. Biophys. Acta 258 (1972) 133-146. [PMID: 4550801]

5. van den Hamer, C.J.A., Morell, A.G. and Scheinberg, H.I. A study of the copper content of β-mercaptopyruvate trans-sulfurase. J. Biol. Chem. 242 (1967) 2514-2516. [PMID: 6026243]

[EC 2.8.1.2 created 1961]

EC 2.8.1.3

Accepted name: thiosulfate—thiol sulfurtransferase

Reaction: thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide

Other name(s): glutathione-dependent thiosulfate reductase; sulfane reductase; sulfane sulfurtransferase

Systematic name: thiosulfate:thiol sulfurtransferase

Comments: The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. L-Cysteine can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111070-24-7

References:

1. Peck, H.D. and Fischer, E. The oxidation of thiosulfate and phosphorylation in extracts of Thiobacillus thioparus. J. Biol. Chem. 237 (1962) 190-197.

2. Sido, B. and Koj, A. Separation of rhodanese and thiosulfate reductase activities in carp liver extracts. Acta Biol. Cracow Ser. Zoo. 15 (1972) 97-103.

3. Uhteg, L.C. and Westley, J. Purification and steady-state kinetic analysis of yeast thiosulfate reductase. Arch. Biochem. Biophys. 195 (1979) 211-222. [PMID: 383018]

[EC 2.8.1.3 created 1982]

EC 2.8.1.4

Accepted name: tRNA uracil 4-sulfurtransferase

Reaction: ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster

Other name(s): thiI (gene name); transfer ribonucleate sulfurtransferase (ambiguous); RNA sulfurtransferase (ambiguous); ribonucleate sulfurtransferase (ambiguous); transfer RNA sulfurtransferase (ambiguous); transfer RNA thiolase (ambiguous); L-cysteine:tRNA sulfurtransferase (incorrect); tRNA sulfurtransferase (ambiguous)

Systematic name: [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine:uracil in tRNA sulfurtransferase

Comments: The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-57-6

References:

1. Abrell, J.W., Kaufman, E.E. and Lipsett, M.N. The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system. J. Biol. Chem. 246 (1971) 294-301. [PMID: 5541999]

2. Hayward, R.S. and Weiss, S.B. RNA thiolase: the enzymatic transfer of sulfur from cysteine to sRNA in Escherichia coli extracts. Proc. Natl. Acad. Sci. USA 55 (1966) 1161-1168. [PMID: 5334200]

3. Lipsett, M.N. and Peterkofsky, A. Enzymatic thiolation of E. coli sRNA. Proc. Natl. Acad. Sci. USA 55 (1966) 1169-1174. [PMID: 5334201]

4. Wong, T., Weiss, S.B., Eliceiri, G.L. and Bryant, J. Ribonucleic acid sulfurtransferase from Bacillus subtilis W168. Sulfuration with β-mercaptopyruvate and properties of the enzyme system. Biochemistry 9 (1970) 2376-2386. [PMID: 4987417]

5. Kambampati, R. and Lauhon, C.T. Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. J. Biol. Chem. 275 (2000) 10727-10730. [PMID: 10753862]

6. Mueller, E.G., Palenchar, P.M. and Buck, C.J. The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA. J. Biol. Chem. 276 (2001) 33588-33595. [PMID: 11443125]

7. Lauhon, C.T., Erwin, W.M. and Ton, G.N. Substrate specificity for 4-thiouridine modification in Escherichia coli. J. Biol. Chem. 279 (2004) 23022-23029. [PMID: 15037613]

8. Neumann, P., Lakomek, K., Naumann, P.T., Erwin, W.M., Lauhon, C.T. and Ficner, R. Crystal structure of a 4-thiouridine synthetase-RNA complex reveals specificity of tRNA U8 modification. Nucleic Acids Res. 42 (2014) 6673-6685. [PMID: 24705700]

9. Liu, Y., Vinyard, D.J., Reesbeck, M.E., Suzuki, T., Manakongtreecheep, K., Holland, P.L., Brudvig, G.W. and Soll, D. A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes. Proc. Natl Acad. Sci. USA 113 (2016) 12703-12708. [PMID: 27791189]

[EC 2.8.1.4 created 1984, modified 2017]

EC 2.8.1.5

Accepted name: thiosulfate—dithiol sulfurtransferase

Reaction: thiosulfate + dithioerythritol = sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized dithioerythritol) + sulfide

Other name(s): thiosulfate reductase; TSR

Systematic name: thiosulfate:dithioerythritol sulfurtransferase

Comments: The enzyme from Chlorella shows very little activity towards monothiols such as glutathione and cysteine (cf. EC 2.8.1.3 thiosulfate—thiolsulfurtransferase). The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S-, and sulfide is spontaneously expelled from this by reaction with the other thiol group. May be identical with EC 2.8.1.1 thiosulfate sulfurtransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9059-49-8

References:

1. Schmidt, A., Erdle, I. and Gamon, B. Isolation and characterization of thiosulfate reductases from the green alga Chlorella fusca. Planta 162 (1984) 243-249.

[EC 2.8.1.5 created 1989, modified 1999]

EC 2.8.1.6

Accepted name: biotin synthase

Reaction: dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin

Other name(s): dethiobiotin:sulfur sulfurtransferase

Systematic name: dethiobiotin:sulfur-(sulfur carrier) sulfurtransferase

Comments: The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical. Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80146-93-6

References:

1. Trainor, D.A., Parry, R.J. and Gitterman, A. Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin. J. Am. Chem. Soc. 102 (1980) 1467-1468.

2. Shiuan, D. and Campbell, A. Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons. Gene 67 (1988) 203-211. [PMID: 2971595]

3. Zhang, S., Sanyal, I., Bulboaca, G.H., Rich, A. and Flint, D.H. The gene for biotin synthase from Saccharomyces cerevisiae: cloning, sequencing, and complementation of Escherichia coli strains lacking biotin synthase. Arch. Biochem. Biophys. 309 (1994) 29-35. [PMID: 8117110]

4. Ugulava, N.B., Gibney, B.R. and Jarrett, J.T. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 40 (2001) 8343-8351. [PMID: 11444981]

5. Berkovitch, F., Nicolet, Y., Wan, J.T., Jarrett, J.T. and Drennan, C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303 (2004) 76-79. [PMID: 14704425]

6. Lotierzo, M., Tse Sum Bui, B., Florentin, D., Escalettes, F. and Marquet, A. Biotin synthase mechanism: an overview. Biochem. Soc. Trans. 33 (2005) 820-823. [PMID: 16042606]

7. Taylor, A.M., Farrar, C.E. and Jarrett, J.T. 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase. Biochemistry 47 (2008) 9309-9317. [PMID: 18690713]

8. Reyda, M.R., Fugate, C.J. and Jarrett, J.T. A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry 48 (2009) 10782-10792. [PMID: 19821612]

[EC 2.8.1.6 created 1999, modified 2006, modified 2011, modified 2014]

EC 2.8.1.7

Accepted name: cysteine desulfurase

Reaction: L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor (overall reaction)
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
(1b) [enzyme]-S-sulfanylcysteine + acceptor = [enzyme]-cysteine + S-sulfanyl-acceptor

For diagram of reaction click here.

Other name(s): IscS; NIFS; NifS; SufS; cysteine desulfurylase

Systematic name: L-cysteine:acceptor sulfurtransferase

Comments: A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 149371-08-4

References:

1. Zheng, L.M., White, R.H., Cash, V.L., Jack, R.F. and Dean, D.R. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90 (1993) 2754-2758. [PMID: 8464885]

2. Mihara, H. and Esaki, N. Bacterial cysteine desulfurases: Their function and mechanisms. Appl. Microbiol. Biotechnol. 60 (2002) 12-23. [PMID: 12382038]

3. Frazzon, J. and Dean, D.R. Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7 (2003) 166-173. [PMID: 12714048]

[EC 2.8.1.7 created 2003, modified 2011]

EC 2.8.1.8

Accepted name: lipoyl synthase

Reaction: protein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin

Other name(s): LS; LipA; lipoate synthase; protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase; protein N6-(octanoyl)lysine:sulfur sulfurtransferase

Systematic name: protein N6-(octanoyl)lysine:sulfur-(sulfur carrier) sulfurtransferase

Comments: This enzyme is a member of the ‘AdoMet radical’ (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet [i.e. S-adenosylmethionine, or S-(5'-deoxyadenosin-5'-yl)methionine], by the addition of an electron from an iron-sulfur centre. The radical is converted into 5'-deoxyadenosine when it abstracts a hydrogen atom from C-6 and C-8, leaving reactive radicals at these positions so that they can add sulfur, with inversion of configuration [4]. This enzyme catalyses the final step in the de-novo biosynthesis of the lipoyl cofactor, with the other enzyme involved being EC 2.3.1.181, lipoyl(octanoyl) transferase. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,5]. An alternative lipoylation pathway involves EC 2.7.7.63, lipoate—protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues) [7].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 189398-80-9

References:

1. Cicchillo, R.M. and Booker, S.J. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J. Am. Chem. Soc. 127 (2005) 2860-2861. [PMID: 15740115]

2. Vanden Boom, T.J., Reed, K.E. and Cronan, J.E., Jr. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J. Bacteriol. 173 (1991) 6411-6420. [PMID: 1655709]

3. Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem. Biol. 10 (2003) 1293-1302. [PMID: 14700636]

4. Cicchillo, R.M., Iwig, D.F., Jones, A.D., Nesbitt, N.M., Baleanu-Gogonea, C., Souder, M.G., Tu, L. and Booker, S.J. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry 43 (2004) 6378-6386. [PMID: 15157071]

5. Jordan, S.W. and Cronan, J.E., Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903-17906. [PMID: 9218413]

6. Miller, J.R., Busby, R.W., Jordan, S.W., Cheek, J., Henshaw, T.F., Ashley, G.W., Broderick, J.B., Cronan, J.E., Jr. and Marletta, M.A. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39 (2000) 15166-15178. [PMID: 11106496]

7. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

[EC 2.8.1.8 created 2006, modified 2014]

EC 2.8.1.9

Accepted name: molybdenum cofactor sulfurtransferase

Reaction: molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor

For diagram of reaction click here.

Glossary: molybdenum cofactor = MoCo = MoO2(OH)Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-κS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2–) phosphate}(dioxo)molybdate

Other name(s): molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase

Systematic name: L-cysteine:molybdenum cofactor sulfurtransferase

Comments: Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.

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

References:

1. Bittner, F., Oreb, M. and Mendel, R.R. ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 40381-40384. [PMID: 11553608]

2. Heidenreich, T., Wollers, S., Mendel, R.R. and Bittner, F. Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J. Biol. Chem. 280 (2005) 4213-4218. [PMID: 15561708]

3. Wollers, S., Heidenreich, T., Zarepour, M., Zachmann, D., Kraft, C., Zhao, Y., Mendel, R.R. and Bittner, F. Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J. Biol. Chem. 283 (2008) 9642-9650. [PMID: 18258600]

[EC 2.8.1.9 created 2011, modified 2015]

EC 2.8.1.10

Accepted name: thiazole synthase

Reaction: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O

For diagram of reaction click here.

Glossary: cThz*-P = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate

Other name(s): thiG (gene name)

Systematic name: 1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase

Comments: H2S can provide the sulfur in vitro. Part of the pathway for thiamine biosynthesis.

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

References:

1. Park, J.H., Dorrestein, P.C., Zhai, H., Kinsland, C., McLafferty, F.W. and Begley, T.P. Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1). Biochemistry 42 (2003) 12430-12438. [PMID: 14567704]

2. Dorrestein, P.C., Zhai, H., McLafferty, F.W. and Begley, T.P. The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS. Chem. Biol. 11 (2004) 1373-1381. [PMID: 15489164]

3. Dorrestein, P.C., Zhai, H., Taylor, S.V., McLafferty, F.W. and Begley, T.P. The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase. J. Am. Chem. Soc. 126 (2004) 3091-3096. [PMID: 15012138]

4. Settembre, E.C., Dorrestein, P.C., Zhai, H., Chatterjee, A., McLafferty, F.W., Begley, T.P. and Ealick, S.E. Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex. Biochemistry 43 (2004) 11647-11657. [PMID: 15362849]

5. Hazra, A., Chatterjee, A. and Begley, T.P. Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction. J. Am. Chem. Soc. 131 (2009) 3225-3229. [PMID: 19216519]

6. Hazra, A.B., Han, Y., Chatterjee, A., Zhang, Y., Lai, R.Y., Ealick, S.E. and Begley, T.P. A missing enzyme in thiamin thiazole biosynthesis: identification of TenI as a thiazole tautomerase. J. Am. Chem. Soc. 133 (2011) 9311-9319. [PMID: 21534620]

[EC 2.8.1.10 created 2011, modified 2016]

EC 2.8.1.11

Accepted name: molybdopterin synthase sulfurtransferase

Reaction: [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + [cysteine desulfurase] + oxidized acceptor

For diagram of reaction click here.

Other name(s): adenylyltransferase and sulfurtransferase MOCS3; Cnx5 (gene name); molybdopterin synthase sulfurylase

Systematic name: persulfurated L-cysteine desulfurase:[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly sulfurtransferase

Comments: The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12, molybdopterin synthase. In the human, the reaction is catalysed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80, molybdopterin-synthase adenylyltransferase, at the N-terminal domain.

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

References:

1. Matthies, A., Nimtz, M. and Leimkuhler, S. Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44 (2005) 7912-7920. [PMID: 15910006]

2. Leimkuhler, S. and Rajagopalan, K.V. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J. Biol. Chem. 276 (2001) 22024-22031. [PMID: 11290749]

3. Hanzelmann, P., Dahl, J.U., Kuper, J., Urban, A., Muller-Theissen, U., Leimkuhler, S. and Schindelin, H. Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Sci. 18 (2009) 2480-2491. [PMID: 19798741]

4. Dahl, J.U., Urban, A., Bolte, A., Sriyabhaya, P., Donahue, J.L., Nimtz, M., Larson, T.J. and Leimkuhler, S. The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J. Biol. Chem. 286 (2011) 35801-35812. [PMID: 21856748]

[EC 2.8.1.11 created 2011, modified 2016]

EC 2.8.1.12

Accepted name: molybdopterin synthase

Reaction: cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O = molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein

For diagram of reaction click here.

Glossary: molybdopterin = H2Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-κS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2–) phosphate}(dioxo)molybdate(2–)
cPMP = cyclic pyranopterin monophosphate = precursor Z = 8-amino-2,12,12-trihydroxy-4a,5a,6,9,11,11a,12,12a-octahydro[1,3,2]dioxaphosphinino[4',5':5,6]pyrano[3,2-g]pteridin-10(4H)-one 2-oxide = 8-amino-2,12,12-trihydroxy-4,4a,5a,6,9,10,11,11a,12,12a-decahydro-[1,3,2]dioxaphosphinino[4',5':5,6]pyrano[3,2-g]pteridine 2-oxide

Other name(s): MPT synthase; thiocarboxylated molybdopterin synthase:cyclic pyranopterin monophosphate sulfurtransferase

Systematic name: thiocarboxylated molybdopterin synthase:cyclic pyranopterin phosphate sulfurtransferase

Comments: Catalyses the synthesis of molybdopterin from cyclic pyranopterin monophosphate. Two sulfur atoms are transferred to cyclic pyranopterin monophosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor. Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur-carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase. The reaction occurs in prokaryotes and eukaryotes.

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

References:

1. Daniels, J.N., Wuebbens, M.M., Rajagopalan, K.V. and Schindelin, H. Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency. Biochemistry 47 (2008) 615-626. [PMID: 18092812]

2. Wuebbens, M.M. and Rajagopalan, K.V. Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. J. Biol. Chem. 278 (2003) 14523-14532. [PMID: 12571226]

[EC 2.8.1.12 created 2011]

EC 2.8.1.13

Accepted name: tRNA-uridine 2-sulfurtransferase

Reaction: a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor

Other name(s): mnmA (gene name)

Systematic name: [protein]-S-sulfanyl-L-cysteine:tRNA (uridine34-2-O)-sulfurtransferase

Comments: The enzyme, found in bacteria, catalyses formation of the 2-thiouridine modification in the wobble position of tRNAGln, tRNALys and tRNAGlu.

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

References:

1. Kambampati, R. and Lauhon, C.T. MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli. Biochemistry 42 (2003) 1109-1117. [PMID: 12549933]

2. Ikeuchi, Y., Shigi, N., Kato, J., Nishimura, A. and Suzuki, T. Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol. Cell 21 (2006) 97-108. [PMID: 16387657]

[EC 2.8.1.13 created 2015]

EC 2.8.1.14

Accepted name: tRNA-5-taurinomethyluridine 2-sulfurtransferase

Reaction: a [protein]-S-sulfanyl-L-cysteine + 5-taurinomethyluridine34 in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 5-taurinomethyl-2-thiouridine34 in tRNA + AMP + diphosphate + acceptor

Other name(s): MTU1 (gene name); SLM3 (gene name); MTO2 (gene name)

Systematic name: [protein]-S-sulfanyl-L-cysteine:tRNA (5-taurinomethyluridine34 2-O)-sulfurtransferase

Comments: The enzyme, found in mitochondria, catalyses formation of 5-taurinomethyl-2-thiouridine in the wobble position of mitochondrial tRNAGln, tRNALys and tRNAGlu.

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

References:

1. Umeda, N., Suzuki, T., Yukawa, M., Ohya, Y., Shindo, H., Watanabe, K. and Suzuki, T. Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases. J. Biol. Chem. 280 (2005) 1613-1624. [PMID: 15509579]

2. Wang, X., Yan, Q. and Guan, M.X. Deletion of the MTO2 gene related to tRNA modification causes a failure in mitochondrial RNA metabolism in the yeast Saccharomyces cerevisiae. FEBS Lett. 581 (2007) 4228-4234. [PMID: 17706197]

[EC 2.8.1.14 created 2015]

EC 2.8.1.15

Accepted name: tRNA-5-methyluridine54 2-sulfurtransferase

Reaction: ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O = AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly

Other name(s): TtuA

Systematic name: [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH:tRNA (5-methyluridine54-2-O)-sulfurtransferase

Comments: The enzyme, found in thermophilic bacteria such as Thermus thermophilus and archaea such as Pyrococcus horikoshii, modifies the ribothymidine (5-methyluridine) residue at position 54 of tRNAs. Contains zinc.

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

References:

1. Shigi, N., Sakaguchi, Y., Suzuki, T. and Watanabe, K. Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures. J. Biol. Chem. 281 (2006) 14296-14306. [PMID: 16547008]

2. Shigi, N., Suzuki, T., Terada, T., Shirouzu, M., Yokoyama, S. and Watanabe, K. Temperature-dependent biosynthesis of 2-thioribothymidine of Thermus thermophilus tRNA. J. Biol. Chem. 281 (2006) 2104-2113. [PMID: 16317006]

3. Nakagawa, H., Kuratani, M., Goto-Ito, S., Ito, T., Katsura, K., Terada, T., Shirouzu, M., Sekine, S., Shigi, N. and Yokoyama, S. Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA. Proteins 81 (2013) 1232-1244. [PMID: 23444054]

4. Chen, M., Narai, S., Omura, N., Shigi, N., Chimnaronk, S., Tanaka, Y. and Yao, M. Crystallographic study of the 2-thioribothymidine-synthetic complex TtuA-TtuB from Thermus thermophilus. Acta Crystallogr. F Struct. Biol. Commun. 72 (2016) 777-781. [PMID: 27710943]

[EC 2.8.1.15 created 2017]


EC 2.8.2 Sulfotransferases

Contents

EC 2.8.2.1 aryl sulfotransferase
EC 2.8.2.2 alcohol sulfotransferase
EC 2.8.2.3 amine sulfotransferase
EC 2.8.2.4 estrone sulfotransferase
EC 2.8.2.5 chondroitin 4-sulfotransferase
EC 2.8.2.6 choline sulfotransferase
EC 2.8.2.7 UDP-N-acetylgalactosamine-4-sulfate sulfotransferase
EC 2.8.2.8 desulfoheparin sulfotransferase
EC 2.8.2.9 tyrosine-ester sulfotransferase
EC 2.8.2.10 Renilla-luciferin sulfotransferase
EC 2.8.2.11 galactosylceramide sulfotransferase
EC 2.8.2.12 deleted identical to EC 2.8.2.8
EC 2.8.2.13 psychosine sulfotransferase
EC 2.8.2.14 bile-salt sulfotransferase
EC 2.8.2.15 steroid sulfotransferase
EC 2.8.2.16 thiol sulfotransferase
EC 2.8.2.17 chondroitin 6-sulfotransferase
EC 2.8.2.18 cortisol sulfotransferase
EC 2.8.2.19 triglucosylalkylacylglycerol sulfotransferase
EC 2.8.2.20 protein-tyrosine sulfotransferase
EC 2.8.2.21 keratan sulfotransferase
EC 2.8.2.22 aryl-sulfate sulfotransferase
EC 2.8.2.23 [heparan sulfate]-glucosamine 3-sulfotransferase 1
EC 2.8.2.24 desulfoglucosinolate sulfotransferase
EC 2.8.2.25 flavonol 3-sulfotransferase
EC 2.8.2.26 quercetin-3-sulfate 3'-sulfotransferase
EC 2.8.2.27 quercetin-3-sulfate 4'-sulfotransferase
EC 2.8.2.28 quercetin-3,3'-bissulfate 7-sulfotransferase
EC 2.8.2.29 [heparan sulfate]-glucosamine 3-sulfotransferase 2
EC 2.8.2.30 [heparan sulfate]-glucosamine 3-sulfotransferase 3
EC 2.8.2.31 petromyzonol sulfotransferase
EC 2.8.2.32 scymnol sulfotransferase
EC 2.8.2.33 N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
EC 2.8.2.34 glycochenodeoxycholate sulfotransferase
EC 2.8.2.35 dermatan 4-sulfotransferase
EC 2.8.2.36 desulfo-A47934 sulfotransferase
EC 2.8.2.37 trehalose 2-sulfotransferase


Entries

EC 2.8.2.1

Accepted name: aryl sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate

Glossary and synonyms entries:
dopamine
3'-phosphoadenylyl sulfate = PAPS

Other name(s): phenol sulfotransferase; sulfokinase; 1-naphthol phenol sulfotransferase; 2-naphtholsulfotransferase; 4-nitrocatechol sulfokinase; arylsulfotransferase; dopamine sulfotransferase; p-nitrophenol sulfotransferase; phenol sulfokinase; ritodrine sulfotransferase; PST

Systematic name: 3'-phosphoadenylyl-sulfate:phenol sulfotransferase

Comments: A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-09-9

References:

1. Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999-1005. [PMID: 6956338]

2. Sekura, R. and Jakoby, W.B. Phenol sulfotransferases. J. Biol. Chem. 254 (1979) 5658-5663. [PMID: 447677]

[EC 2.8.2.1 created 1961, modified 1980]

EC 2.8.2.2

Accepted name: alcohol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): hydroxysteroid sulfotransferase; 3β-hydroxy steroid sulfotransferase; δ5-3β-hydroxysteroid sulfokinase; 3-hydroxysteroid sulfotransferase; HST; 5α-androstenol sulfotransferase; cholesterol sulfotransferase; dehydroepiandrosterone sulfotransferase; estrogen sulfokinase; estrogen sulfotransferase; steroid alcohol sulfotransferase; steroid sulfokinase; steroid sulfotransferase; sterol sulfokinase; sterol sulfotransferase; alcohol/hydroxysteroid sulfotransferase; 3β-hydroxysteroid sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:alcohol sulfotransferase

Comments: Primary and secondary alcohols, including aliphatic alcohols, ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid sulfotransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-76-2

References:

1. Lyon, E.S. and Jakoby, W.B. The identity of alcohol sulfotransferases with hydroxysteroid sulfotransferases. Arch. Biochem. Biophys. 202 (1980) 474-481. [PMID: 6935986]

2. Lyon, E.S., Marcus, C.J., Wang, J.-L. and Jakoby, W.B. Hydroxysteroid sulfotransferase. Methods Enzymol. 77 (1981) 206-213. [PMID: 6173569]

[EC 2.8.2.2 created 1961, modified 1980]

EC 2.8.2.3

Accepted name: amine sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + an amine = adenosine 3',5'-bisphosphate + a sulfamate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): arylamine sulfotransferase; amine N-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:amine N-sulfotransferase

Comments: A large number of primary and secondary amines can act as acceptors, including aniline, 2-naphthylamine, cyclohexylamine and octylamine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-08-8

References:

1. Ramaswamy, S.G. and Jakoby, W.B. Amine N-sulfotransferase. J. Biol. Chem. 262 (1987) 10039-10043. [PMID: 3475273]

2. Roy, A.B. The enzymic synthesis of aryl sulphamates. Biochem. J. 74 (1960) 49-56.

[EC 2.8.2.3 created 1965]

EC 2.8.2.4

Accepted name: estrone sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: 3'-phosphoadenylyl sulfate-estrone 3-sulfotransferase; estrogen sulfotransferase; estrogen sulphotransferase; oestrogen sulphotransferase; 3'-phosphoadenylylsulfate:oestrone sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:estrone 3-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-06-6

References:

1. Adams, J.B. and Poulos, A. Enzymic synthesis of steroid sulphates. 3. Isolation and properties of estrogen sulphotransferase of bovine adrenal glands. Biochim. Biophys. Acta 146 (1967) 493-508. [PMID: 4965224]

2. Rozhin, J., Zemlicka, J. and Brooks, S.C. Studies on bovine adrenal estrogen sulfotransferase. Inhibition and possible involvement of adenine-estrogen stacking. J. Biol. Chem. 252 (1967) 7214-7220.

3. Adams, J.B., Ellyard, R.K. and Low, J. Enzymic synthesis of steroid sulphates. IX. Physical and chemical properties of purified oestrogen sulphotransferase from bovine adrenal glands. The nature of its isoenzymic forms and a proposed model to explain its wave-like kinetics. Biochem. Biophys. Acta 370 (1974) 160-188.

[EC 2.8.2.4 created 1965]

EC 2.8.2.5

Accepted name: chondroitin 4-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: chondroitin sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:chondroitin 4'-sulfotransferase

Comments: The sulfation takes place at the 4-position of N-acetyl-galactosamine residues of chondroitin. Not identical with EC 2.8.2.17 chondroitin 6-sulfotransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83589-04-2

References:

1. Habuchi, O. and Miyashita, N. Separation and characterization of chondroitin 6-sulfotransferase and chondroitin 4-sulfotransferase from chick embryo cartilage. Biochim. Biophys. Acta 717 (1982) 414-421. [PMID: 6957247]

2. Nakanishi, Y., Otsu, K. and Suzuki, S. Enzymatic transfer of galactosyl phosphate from UDP-galactose to UDP-N-acetylglucosamine. FEBS Lett. 151 (1983) 15-18. [PMID: 6130977]

3. Nakanishi, Y., Shimizu, M., Otsu, K., Kato, S., Tsuji, M. and Suzuki, S. A terminal 6-sulfotransferase catalyzing a synthesis of N-acetylgalactosamine 4,6-bissulfate residue at the nonreducing terminal position of chondroitin sulfate. J. Biol. Chem. 256 (1981) 5443-5449. [PMID: 6787041]

4. Suzuki, S. and Strominger, J.L. Enzymatic sulfation of mucopolysaccharides in hen oviduct. I. Transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to mucopolysaccharides. J. Biol. Chem. 235 (1960) 257-266.

5. Suzuki, S. and Strominger, J.L. Enzymatic sulfation of mucopolysaccharides in hen oviduct. II. Mechanism of the reaction studied with oligosaccharides and monosaccharides as acceptors. J. Biol. Chem. 235 (1960) 267-273.

6. Suzuki, S. and Strominger, J.L. Enzymatic sulfation of mucopolysaccharides in hen oviduct. III. Mechanism of sulfation of chondroitin and chondroitin sulfate A. J. Biol. Chem. 235 (1960) 274-276.

[EC 2.8.2.5 created 1965, modified 1986]

EC 2.8.2.6

Accepted name: choline sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + choline = adenosine 3',5'-bisphosphate + choline sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: choline sulphokinase

Systematic name: 3'-phosphoadenylyl-sulfate:choline sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9047-23-8

References:

1. Orsi, B.A. and Spencer, B. Choline sulphokinase (sulphotransferase). J. Biochem. (Tokyo) 56 (1964) 81-91.

[EC 2.8.2.6 created 1972]

EC 2.8.2.7

Accepted name: UDP-N-acetylgalactosamine-4-sulfate sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + UDP-N-acetyl-D-galactosamine 4-sulfate = adenosine 3',5'-bisphosphate + UDP-N-acetyl-D-galactosamine 4,6-bissulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase; uridine diphospho-N-acetylgalactosamine 4-sulfate sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate 6-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-32-3

References:

1. Harada, T., Shimizu, S., Nakanishi, Y. and Suzuki, S. Enzymatic transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to uridine diphosphate N-acetylgalactosamine 4-sulfate. J. Biol. Chem. 242 (1967) 2288-2290. [PMID: 6022874]

[EC 2.8.2.7 created 1972]

EC 2.8.2.8

Accepted name: [heparan sulfate]-glucosamine N-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: heparin N-sulfotransferase; 3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase; PAPS:N-desulfoheparin sulfotransferase; PAPS:DSH sulfotransferase; N-HSST; N-heparan sulfate sulfotransferase; heparan sulfate N-deacetylase/N-sulfotransferase; heparan sulfate 2-N-sulfotransferase; heparan sulfate N-sulfotransferase; heparan sulfate sulfotransferase; N-desulfoheparin sulfotransferase; desulfoheparin sulfotransferase; 3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase; heparitin sulfotransferase; 3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfotransferase

Comments: The enzyme also catalyses the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-75-9

References:

1. Suzuki, S., Trenn, R.H. and Strominger, J.L. Separation of specific mucopolysaccharide sulfotransferases. Biochim. Biophys. Acta 50 (1961) 169-174.

2. Eisenman, R.A., Balasubramanian, A.S. and Marx, W. 3'-Phosphoadenylylsulfate:N-desulfoheparin sulfotransferase associated with a postmicrosomal particulate mastocytoma fraction. Arch. Biochem. Biophys. 119 (1967) 387-397. [PMID: 4964017]

3. Johnson, A.H. and Baker, J.R. The enzymatic sulphation of heparan sulphate by hen's uterus. Biochim. Biophys. Acta 320 (1973) 341-351. [PMID: 4270798]

[EC 2.8.2.8 created 1972, modified 2001 (EC 2.8.2.12 created 1972, incorporated 2001)]

EC 2.8.2.9

Accepted name: tyrosine-ester sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: aryl sulfotransferase IV; L-tyrosine methyl ester sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase

Comments: Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1 aryl sulfotransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-56-5

References:

1. Duffel, M. and Jakoby, W.B. On the mechanism of aryl sulfotransferase. J. Biol. Chem. 256 (1981) 11123-111277. [PMID: 6945304]

2. Mattock, P. and Jones, J.G. Partial purification and properties of an enzyme from rat liver that catalyses the sulphation of L-tyrosyl derivatives. Biochem. J. 116 (1970) 797-803. [PMID: 5441369]

3. Sekura, R. and Jakoby, W.B. Aryl sulfotransferase IV from rat liver. Arch. Biochem. Biophys. 211 (1981) 352-359. [PMID: 6946725]

[EC 2.8.2.9 created 1972, deleted 1980, reinstated 1984]

EC 2.8.2.10

Accepted name: Renilla-luciferin sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + Renilla luciferin = adenosine 3',5'-bisphosphate + luciferyl sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): luciferin sulfotransferase; luciferin sulfokinase; luciferin sulfokinase (3'-phosphoadenylyl sulfate:luciferin sulfotransferase)

Systematic name: 3'-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase

Comments: The product may be identical with Watasenia luciferin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-33-4

References:

1. Cormier, M.J., Hori, K. and Karkhanis, Y.D. Studies on the bioluminescence of Renilla reniformis. VII. Conversion of luciferin into luciferyl sulfate by luciferin sulfokinase. Biochemistry 9 (1970) 1184-1189. [PMID: 4392153]

[EC 2.8.2.10 created 1972, modified 1982]

EC 2.8.2.11

Accepted name: galactosylceramide sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: GSase; 3'-phosphoadenosine-5'-phosphosulfate-cerebroside sulfotransferase; galactocerebroside sulfotransferase; galactolipid sulfotransferase; glycolipid sulfotransferase; glycosphingolipid sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:galactosylceramide 3'-sulfotransferase

Comments: Also acts on lactosylceramide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9081-06-5

References:

1. McKhann, G.M., Levy, R. and Ho, W. Metabolism of sulfatides. I. The effect of galactocerebrosides on the synthesis of sulfatides. Biochem. Biophys. Res. Commun. 20 (1965) 109-113. [PMID: 5850675]

2. Sakakibara, N., Gasa, S., Kamio, K., Makita, A. and Koyanagi, T. Association of elevated sulfatides and sulfotransferase activities with human renal cell carcinoma. Cancer Res. 49 (1989) 335-339. [PMID: 2562926]

[EC 2.8.2.11 created 1972, modified 1976]

[EC 2.8.2.12 Deleted entry: heparitin sulfotransferase. Enzyme identical to EC 2.8.2.8, [heparan sulfate]-glucosamine N-sulfotransferase (EC 2.8.2.12 created 1972, deleted 2001)]

EC 2.8.2.13

Accepted name: psychosine sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + galactosylsphingosine = adenosine 3',5'-bisphosphate + psychosine sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: PAPS:psychosine sulphotransferase; 3'-phosphoadenosine 5'-phosphosulfate-psychosine sulphotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:galactosylsphingosine sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37259-76-0

References:

1. Nussbaum, J.-L. and Mandel, P. Enzymic synthesis of psychosine sulphate. J. Neurochem. 19 (1972) 1789-1802. [PMID: 5042474]

[EC 2.8.2.13 created 1976]

EC 2.8.2.14

Accepted name: bile-salt sulfotransferase

Reaction: (1) 3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate

(2) 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate

For diagram click here or here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS
glycolithocholate sulfate = N-(3α-sulfooxy-5β-cholan-24-oyl)glycine

Other name(s): BAST I; bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase; bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase; bile acid sulfotransferase I; glycolithocholate sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase

Comments: The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5β-bile acid glycolithocholate, deoxycholate, 3β-hydroxy-5-cholenoate and dehydroepiandrosterone (3β-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65802-92-8

References:

1. Chen, L.-J., Bolt, R.J. and Admirand, W.H. Enzymatic sulfation of bile salts. Partial purification and characterization of an enzyme from rat liver that catalyzes the sulfation of bile salts. Biochim. Biophys. Acta 480 (1977) 219-227. [PMID: 831833]

2. Barnes, S., Waldrop, R., Crenshaw, J., King, R.J. and Taylor, K.B. Evidence for an ordered reaction mechanism for bile salt: 3'phosphoadenosine-5'-phosphosulfate: sulfotransferase from rhesus monkey liver that catalyzes the sulfation of the hepatotoxin glycolithocholate. J. Lipid Res. 27 (1986) 1111-1123. [PMID: 3470420]

3. Barnes, S., Buchina, E.S., King, R.J., McBurnett, T. and Taylor, K.B. Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic properties. J. Lipid Res. 30 (1989) 529-540. [PMID: 2754334]

4. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]

[EC 2.8.2.14 created 1978, modified 2005]

EC 2.8.2.15

Accepted name: steroid sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: steroid alcohol sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase

Comments: Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9032-76-2

References:

1. Adams, J.B. and McDonald, D. Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals. Biochim. Biophys. Acta 615 (1980) 275-278. [PMID: 6932974]

[EC 2.8.2.15 created 1984]

EC 2.8.2.16

Accepted name: thiol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: phosphoadenylylsulfate-thiol sulfotransferase; PAPS sulfotransferase; adenosine 3'-phosphate 5'-sulphatophosphate sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:thiol S-sulfotransferase

Comments: Also acts on dithiols; substrates include glutathione, dithioerythritol and 2,3-mercaptopropanol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70356-45-5

References:

1. Schmidt, A. The adenosine-5'-phosphosulfate sulfotransferase from spinach (Spinacea oleracea L.). Stabilization, partial purification, and properties. Planta 130 (1976) 257-263.

2. Schmidt, A. and Christen, U. A PAPS-dependent sulfotransferase in Cyanophora paradoxa inhibited by 5'-AMP, 5'-ADP and APS. Z. Naturforsch. C: Biosci. 34 (1979) 222-228.

3. Tsang, M. L.-S. and Schiff, J.A. Studies of sulfate utilization by algae. 17. Reactions of the adenosine 5'-phosphosulfate (APS) sulfotransferase from Chlorella and studies of model reactions which explain the diversity of side products with thiols. Plant Cell Physiol. 17 (1976) 1209-1220.

[EC 2.8.2.16 created 1984]

EC 2.8.2.17

Accepted name: chondroitin 6-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: chondroitin 6-O-sulfotransferase; 3'-phosphoadenosine 5'-phosphosulfate (PAPS):chondroitin sulfate sulfotransferase; terminal 6-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:chondroitin 6'-sulfotransferase

Comments: The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin. Not identical with EC 2.8.2.5 chondroitin 4-sulfotransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37292-93-6

References:

1. Habuchi, O. and Miyashita, N. Separation and characterization of chondroitin 6-sulfotransferase and chondroitin 4-sulfotransferase from chick embryo cartilage. Biochim. Biophys. Acta 717 (1982) 414-421. [PMID: 6957247]

[EC 2.8.2.17 created 1986]

EC 2.8.2.18

Accepted name: cortisol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + cortisol = adenosine 3',5'-bisphosphate + cortisol 21-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): glucocorticosteroid sulfotransferase; glucocorticoid sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:cortisol 21-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 59782-20-6

References:

1. Singer, S.S. and Brill, B. Enzymatic sulfation of steroids. XVII. The properties of the glucocorticoid sulfotransferase activity of guinea pig liver cytosol. Biochim. Biophys. Acta 712 (1982) 590-596. [PMID: 6957246]

2. Singer, S.S., Giera, D., Johnson, J. and Sylvester, S. Enzymatic sulfation of steroids: I. The enzymatic basis for the sex difference in cortisol sulfation by rat liver preparations. Endocrinology 98 (1976) 963-974. [PMID: 1278101]

[EC 2.8.2.18 created 1986]

EC 2.8.2.19

Accepted name: triglucosylalkylacylglycerol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + α-D-glucosyl-(1→6)-α-D-glucosyl-(1→6)-α-D-glucosyl-(1→3)-1-O-alkyl-2-O-acylglycerol = adenosine 3',5'-bisphosphate + 6-sulfo-α-D-glucosyl-(1→6)-α-D-glucosyl-(1→6)-α-D-glucosyl-(1→3)-1-O-alkyl-2-O-acylglycerol

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: triglucosylmonoalkylmonoacyl sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol 6-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83589-05-3

References:

1. Liau, Y.H., Zdebska, E., Slomiany, A. and Slomiany, B.L. Biosynthesis in vitro of a sulfated triglucosyl monoalkylmonoacylglycerol by rat gastric mucosa. J. Biol. Chem. 257 (1982) 12019-12023. [PMID: 6956577]

[EC 2.8.2.19 created 1986]

EC 2.8.2.20

Accepted name: protein-tyrosine sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): tyrosylprotein sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase

Comments: The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 87588-33-8

References:

1. Lee, R.W.H. and Huttner, W.B. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase. J. Biol. Chem. 258 (1983) 11326-11334. [PMID: 6577005]

[EC 2.8.2.20 created 1986]

EC 2.8.2.21

Accepted name: keratan sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: 3'-phosphoadenylyl keratan sulfotransferase; keratan sulfate sulfotransferase; 3'-phosphoadenylylsulfate:keratan sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:keratan 6'-sulfotransferase

Comments: Sulfation takes place at the 6-position of galactosyl and N-acetylglucosaminyl residues in keratan, a proteoglycan. Not identical with EC 2.8.2.5 (chondroitin 4-sulfotransferase), EC 2.8.2.6 (choline sulfotransferase) or EC 2.8.2.17 (chondroitin 6-sulfotransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62168-79-0

References:

1. Ruter, E.-R. and Kresse, H. Partial purification and characterization of 3'-phosphoadenylylsulfate:keratan sulfate sulfotransferases. J. Biol. Chem. 259 (1984) 11771-11776. [PMID: 6592165]

[EC 2.8.2.21 created 1989]

EC 2.8.2.22

Accepted name: aryl-sulfate sulfotransferase

Reaction: an aryl sulfate + a phenol = a phenol + an aryl sulfate

Other names: arylsulfate-phenol sulfotransferase; arylsulfotransferase; ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase

Systematic name: aryl-sulfate:phenol sulfotransferase

Comments: The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+ [1]. Unlike EC 2.8.2.9, tyrosine-ester sulfotransferase and EC 2.8.2.1, aryl sulfotransferase, the enzyme does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate [1]. The level of sulfation of polyphenols depends on the positions of the hydroxyl groups [3-5]. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors [2]. The reaction proceeds according to a ping pong bi bi mechanism [6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 158254-86-5

References:

1. Kim, D.-H., Konishi, L. and Kobashi, K. Purification, characterization and reaction mechanism of novel arylsulfotransferase obtained from an anaerobic bacterium of human intestine. Biochim. Biophys. Acta 872 (1986) 33-41. [PMID: 3460636]

2. Kobashi, K., Kim, D.-H. and Morikawa, T. A novel type of arylsulfotransferase. J. Protein Chem. 6 (1987) 237-244.

3. Koizumi, M., Shimizu, M. and Kobashi, K. Enzymatic sulfation of quercetin by arylsulfotransferase from a human intestinal bacterium. Chem Pharm Bull (Tokyo) 38 (1990) 794-796. [PMID: 2347024]

4. Koizumi, M., Akao, T., Kadota, S., Kikuchi, T., Okuda, T. and Kobashi, K. Enzymatic sulfation of polyphenols related to tannins by arylsulfotransferase. Chem Pharm Bull (Tokyo) 39 (1991) 2638-2643. [PMID: 1806284]

5. Konishi-Imamura, L., Sato, M., Dohi, K., Kadota, S., Namba, T. and Kobashi, K. Enzymatic sulfation of glycosides and their corresponding aglycones by arylsulfate sulfotransferase from a human intestinal bacterium. Biol. Pharm. Bull. 17 (1994) 1018-1022. [PMID: 7820100]

6. Lee, N.S., Kim, B.T., Kim, D.H. and Kobashi, K. Purification and reaction mechanism of arylsulfate sulfotransferase from Haemophilus K-12, a mouse intestinal bacterium. J. Biochem. 118 (1995) 796-801. [PMID: 8576095]

7. Kim, B., Hyun, Y.J., Lee, K.S., Kobashi, K. and Kim, D.H. Cloning, expression and purification of arylsulfate sulfotransferase from Eubacterium A-44. Biol. Pharm. Bull. 30 (2007) 11-14. [PMID: 17202651]

[EC 2.8.2.22 created 1990]

EC 2.8.2.23

Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 1

Reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here

Other name(s): heparin-glucosamine 3-O-sulfotransferase; 3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase; glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 1 (3-OST-1, HS3ST1)

Systematic name: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase

Comments: This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3)] by being the most selective for a precursor of the antithrombin-binding site. It has a minimal acceptor sequence of: → GlcNAc6S→ GlcA→ GlcN2S*±6S→ IdoA2S→ GlcN2S→ , the asterisk marking the target (symbols as in 2-Carb-38 using ± to mean the presence or absence of a substituent, and > to separate a predominant structure from a minor one. Thus Glc(N2S>NAc) means a residue of glucosamine where the N carries a sulfo group mainly but occasionally an acetyl group.) [1-4]. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. These precursors are variants of the consensus sequence: → Glc(N2S>NAc)±6S→ GlcA→ GlcN2S*±6S→ GlcA>IdoA±2S→ Glc(N2S/NAc)±6S→ [5]. If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA [6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 183257-54-7

References:

1. Kusche, M., Backström, G., Riesenfeld, J., Pepitou, M., Choay, J. and Lindahl, U. Biosynthesis of heparin. O-Sulfation of the antithrombin-binding region. J. Biol. Chem. 263 (1988) 15474-15484. [PMID: 3139669]

2. Shworak, N.W., Fritze, L.M.S., Liu, J., Butler, L.D. and Rosenberg, R.D. Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting activity which modifies a nonlimiting precursor pool. J. Biol. Chem. 271 (1996) 27063-27071. [PMID: 8900197]

3. Liu, J., Shworak, N.W., Fritze, L.M.S., Edelberg, J.M. and Rosenberg, R.D. Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 271 (1996) 27072-27082. [PMID: 8900198]

4. Shworak, N.W., Liu, J., Fritze, L.M.S., Schwartz, J.J., Zhang, L., Logeart, D. and Rosenberg, R.D. Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 272 (1997) 28008-28019. [PMID: 9346953]

5. Zhang, L., Yoshida, K., Liu, J. and Rosenberg, R.D. Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells. J. Biol. Chem. 274 (1999) 5681-5691 [PMID: 10026187]

6. Zhang, L., Lawrence, R., Schwartz, J.J., Bai, X., Wei., G, Esko, J.D. and Rosenberg, R.D. The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate. J. Biol. Chem. 276 (2001) 28806-28813. [PMID: 11375390]

[EC 2.8.2.23 created 1992, modified 2001]

EC 2.8.2.24

Accepted name: desulfoglucosinolate sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: PAPS-desulfoglucosinolate sulfotransferase; 3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:desulfoglucosinolate sulfotransferase

Comments: Involved with EC 2.4.1.195 thiohydroximate β-D-glucosyltransferase, in the biosynthesis of thioglycosides in cruciferous plants.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-85-4

References:

1. Jain, J.C., Reed, D.W., Groot Wassink, J.W.D. and Underhill, E.W. A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species. Anal. Biochem. 178 (1989) 137-140. [PMID: 2524977]

[EC 2.8.2.24 created 1992]

EC 2.8.2.25

Accepted name: flavonol 3-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Systematic name: 3'-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase

Comments: Also acts on some other flavonol aglycones.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121855-10-5

References:

1. Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977-981.

[EC 2.8.2.25 created 1992]

EC 2.8.2.26

Accepted name: quercetin-3-sulfate 3'-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,3'-bissulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: flavonol 3'-sulfotransferase; 3'-Sulfotransferase; PAPS:flavonol 3-sulfate 3'-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 3'-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121855-11-6

References:

1. Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977-981.

[EC 2.8.2.26 created 1992]

EC 2.8.2.27

Accepted name: quercetin-3-sulfate 4'-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,4'-bissulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: flavonol 4'-sulfotransferase; PAPS:flavonol 3-sulfate 4'-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 4'-sulfotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121855-12-7

References:

1. Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977-981.

[EC 2.8.2.27 created 1992]

EC 2.8.2.28

Accepted name: quercetin-3,3'-bissulfate 7-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate = adenosine 3',5'-bisphosphate + quercetin 3,7,3'-trissulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other names: flavonol 7-sulfotransferase; 7-sulfotransferase; PAPS:flavonol 3,3'/3,4'-disulfate 7-sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:quercetin-3,3'-bissulfate 7-sulfotransferase

Comments: Quercetin 3,4'-bissulfate can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121855-13-8

References:

1. Varin, L. Enzymatic synthesis of sulfated flavonoids in Flaveria spp. Bull. Liaison-Groupe Polyphenols 14 (1988) 248-257.

[EC 2.8.2.28 created 1992]

EC 2.8.2.29

Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 2

Reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here

Other name(s): glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 2 (3-OST-2, HS3ST2)

Systematic name: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase

Comments: This enzyme sulfates the residues marked with an asterisk in sequences containing at least → IdoA2S→ GlcN*→ or → GlcA2S→ GlcN*→ (symbols as in 2-Carb-38). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.

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

References:

1. Shworak, N.W., Liu, J., Petros, L.M., Copeland, N.G., Jenkins N.A. and Rosenberg, R.D. Diversity of the extensive heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) multigene family. J. Biol. Chem. 274 (1999) 5170-5184. [PMID: 9988767]

2. Liu, J., Shworak, N.W., Sina, P., Schwartz, J.J., Zhang, L., Fritze, L.M.S. and Rosenberg, R.D. Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 274 (1999) 5185-5192. [PMID: 9988768]

[EC 2.8.2.29 created 2001]

EC 2.8.2.30

Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 3

Reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here

Other name(s): glucosaminyl 3-O-sulfotransferase 3a, 3b; heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A; isoform/isozyme 3a and 3b (3-OST-3A, 3-OST-3B, HS3ST3A, HS3ST3B)

Systematic name: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase

Comments: Two major substrates contain the tetrasaccharides: → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN*→ and → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN6S*→ (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].

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

References:

1. Liu, J., Shriver, Z., Blaiklock, P., Yoshida, K., Sasisekharan, R. and Rosenberg, R.D. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A sulfates N-unsubstituted glucosamine. J. Biol. Chem. 274 (1999) 38155-38162. [PMID: 10608887]

2. Shukla, D., Liu, J., Blaiklock, P., Shworak, N.W., Bai, X., Esko, J.D., Cohen, G.H., Eisenberg, R.J., Rosenberg, R.D. and Spear, P.G. A novel role for 3-O-sulfated heparan sulfate in Herpes simplex virus 1 entry. Cell 99 (1999) 13-22. [PMID: 10520990]

3. Shworak, N.W., Liu, J., Petros, L.M., Copeland, N.G., Jenkins N.A. and Rosenberg, R.D. Diversity of the extensive heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) multigene family. J. Biol. Chem. 274 (1999) 5170-5184. [PMID: 9988767]

4. Liu, J., Shworak, N.W., Sina, P., Schwartz, J.J., Zhang, L., Fritze, L.M.S. and Rosenberg, R.D. Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 274 (1999) 5185-5192. [PMID: 9988768]

[EC 2.8.2.30 created 2001]

EC 2.8.2.31

Accepted name: petromyzonol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + 5α-cholan-3α,7α,12α,24-tetrol = adenosine 3',5'-bisphosphate + 5α-cholan-3α,7α,12α-triol 24-sulfate

For diagram click here.

Glossary: petromyzonol = 5α-cholan-3α,7α,12α,24-tetrol
3'-phosphoadenylyl sulfate = PAPS

Other name(s): PZ-SULT

Systematic name: 3'-phosphoadenylyl-sulfate:5α-cholan-3α,7α,12α,24-tetrol sulfotransferase

Comments: The enzyme from the lamprey Petromyzon marinus can also use the corresponding 3-ketone as a substrate. It is stereoselective (5α-cholane) and regioselective, exhibiting a preference for an hydroxy group at C-24. The enzyme is inactive when allocholic acid, which has a carboxy group at C-24, is used as a substrate.

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

References:

1. Venkatachalam, K.V., Llanos, D.E., Karami, K.J. and Malinovskii, V.A. Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver. J. Lipid Res. 45 (2004) 486-495. [PMID: 14657197]

[EC 2.8.2.31 created 2004]

EC 2.8.2.32

Accepted name: scymnol sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + 5β-scymnol = adenosine 3',5'-bisphosphate + 5β-scymnol sulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS
5β-scymnol sulfate = (24R,25S)-3α,7α,12α,24,27-pentahydroxy-5β-cholestan-26-yl sulfate
5α-cyprinol = 5α-cholestane-3α,7α,12α,26,27-pentol

Other names: 3'-phosphoadenosine 5'-phosphosulfate:5β-scymnol sulfotransferase

Systematic name: 3′-phosphoadenylyl sulfate:5β-scymnol sulfotransferase

å Comments: The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C27 bile salts 5β-scymnol (the natural bile salt) and 5α-cyprinol (the carp bile salt). Enzyme activity is activated by Mg2+ but inhibited by the product 5β-scymnol sulfate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 220581-70-4

References:

1. Macrides, T.A., Faktor, D.A., Kalafatis, N. and Amiet, R.G. Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyses the sulfation of the shark bile steroid 5β-scymnol. Comp. Biochem. Physiol. Part B 107 (1994) 461-469. [PMID: 7749614]

2. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. Investigation of 5β-scymnol sulfotransferase from the kidney and testes of Heterodontus portusjacksoni. Comp. Biochem. Physiol. Part B 121 (1998) 243-249.

3. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. 5β-Scymnol sulfotransferase isolated from the tissues of an Australian shark species. Comp. Biochem. Physiol. Part B 121 (1998) 299-307.

4. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. 5β-scymnol sulfotransferase isolated from the liver of two Australian ray species. Comp. Biochem. Physiol. Part B 121 (1998) 341-348.

[EC 2.8.2.32 created 2005]

EC 2.8.2.33

Accepted name: N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase

Reaction: (1) 3-phospho-5-adenylyl sulfate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine = adenosine 3',5'-bisphosphate + [dermatan]-4,6-di-O-sulfo-N-acetyl-D-galactosamine
(2) 3-phospho-5-adenylyl sulfate + [chondroitin]-4-O-sulfo-N-acetyl-D-galactosamine = adenosine 3',5'-bisphosphate + [chondroitin]-4,6-di-O-sulfo-N-acetyl-D-galactosamine

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): GalNAc4S-6ST; CHST15 (gene name)

Systematic name: 3'-phosphoadenylyl-sulfate:[dermatan]-4-O-sulfo-N-acetyl-D-galactosamine 6-O-sulfotransferase

Comments: The enzyme is activated by divalent cations and reduced glutathione. The enzyme from human transfers sulfate to position 6 of both internal residues and non-reducing terminal GalNAc 4-sulfate residues of chondroitin sulfate and dermatan sulfate. Oligosaccharides derived from chondroitin sulfate also serve as acceptors but chondroitin sulfate E, keratan sulfate and heparan sulfate do not. Differs from EC 2.8.2.17, chondroitin 6-sulfotransferase, in being able to use both chondroitin and dermatan as effective substrates

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 242469-38-1

References:

1. Ito, Y. and Habuchi, O. Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage. J. Biol. Chem. 275 (2000) 34728-34736. [PMID: 10871629]

2. Ohtake, S., Ito, Y., Fukuta, M. and Habuchi, O. Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene. J. Biol. Chem. 276 (2001) 43894-43900. [PMID: 11572857]

[EC 2.8.2.33 created 2005, modified 2010]

EC 2.8.2.34

Accepted name: glycochenodeoxycholate sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate

For diagram click here.

Glossary: 3'-phosphoadenylyl sulfate = PAPS
glycochenodeoxycholate 7-sulfate = N-(3α-hydroxy-7α-sulfooxy-5β-cholan-24-oyl)glycine

Other name(s): bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase; bile acid:PAPS:sulfotransferase; BAST

Systematic name: 3'-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase

Comments: The enzyme specifically sulfates glycochenodeoxycholate at the 7α-position (see also EC 2.8.2.14 bile-salt sulfotransferase). The monohydroxy bile acids glycolithocholate, chenodeoxycholate and ursodeoxycholate act as inhibitors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72668-90-7

References:

1. Barnes, S., Burhol, P.G., Zander, R., Haggstrom, G., Settine, R.L. and Hirschowitz, B.I. Enzymatic sulfation of glycochenodeoxycholic acid by tissue fractions from adult hamsters. J. Lipid Res. 20 (1979) 952-959. [PMID: 533830]

2. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]

[EC 2.8.2.34 created 2005]

EC 2.8.2.35

Accepted name: dermatan 4-sulfotransferase

Reaction: 3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine = adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase; dermatan-4-sulfotransferase-1; dermatan-4-sulfotransferase 1; D4ST-1; dermatan N-acetylgalactosamine 4-O-sulfotransferase; CHST14 protein; CHST14

Systematic name: 3'-phospho-5'-adenylyl sulfate:[dermatan]-N-acetyl-D-galactosamine 4-sulfotransferase

Comments: The sulfation takes place at the 4-position of N-acetylgalactosamine residues of dermatan. D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAα(1,3)GalNAcβ(1,4) that is flanked by GlcUAβ(1,3)GalNAcβ(1,4) as compared with IdoUAα(1,3)GalNAcβ(1,4) flanked by IdoUAα(1,3)GalNAcβ(1,4) [1].

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

References:

1. Evers, M.R., Xia, G., Kang, H.G., Schachner, M. and Baenziger, J.U. Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. J. Biol. Chem. 276 (2001) 36344-36353. [PMID: 11470797]

2. Mikami, T., Mizumoto, S., Kago, N., Kitagawa, H. and Sugahara, K. Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. J. Biol. Chem. 278 (2003) 36115-36127. [PMID: 12847091]

3. Pacheco, B., Maccarana, M. and Malmstrom, A. Dermatan 4-O-sulfotransferase 1 is pivotal in the formation of iduronic acid blocks in dermatan sulfate. Glycobiology 19 (2009) 1197-1203. [PMID: 19661164]

4. Mitsunaga, C., Mikami, T., Mizumoto, S., Fukuda, J. and Sugahara, K. Chondroitin sulfate/dermatan sulfate hybrid chains in the development of cerebellum. Spatiotemporal regulation of the expression of critical disulfated disaccharides by specific sulfotransferases. J. Biol. Chem. 281 (2006) 18942-18952. [PMID: 16702220]

[EC 2.8.2.35 created 2010]

EC 2.8.2.36

Accepted name: desulfo-A47934 sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + desulfo-A47934 = adenosine 3',5'-bisphosphate + A47934

Glossary: desulfo-A47934 = LY 154989 = 7-demethyl-64-O-demethyl-19-deoxy-22,31,45-trichloro-11-sulfo-ristomycin A aglycone

Other name(s): StaL

Systematic name: 3'-phosphoadenylyl-sulfate:desulfo-A47934 sulfotransferase

Comments: The enzyme from the bacterium Streptomyces toyocaensis catalyses the final step in the biosynthesis of the glycopeptide antibiotic A47934, a naturally occuring antibiotic of the vancomycin group.

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

References:

1. Lamb, S.S., Patel, T., Koteva, K.P. and Wright, G.D. Biosynthesis of sulfated glycopeptide antibiotics by using the sulfotransferase StaL. Chem. Biol. 13 (2006) 171-181. [PMID: 16492565]

2. Shi, R., Lamb, S.S., Bhat, S., Sulea, T., Wright, G.D., Matte, A. and Cygler, M. Crystal structure of StaL, a glycopeptide antibiotic sulfotransferase from Streptomyces toyocaensis. J. Biol. Chem. 282 (2007) 13073-13086. [PMID: 17329243]

[EC 2.8.2.36 created 2014]

EC 2.8.2.37

Accepted name: trehalose 2-sulfotransferase

Reaction: 3'-phosphoadenylyl sulfate + α,α-trehalose = adenosine 3',5'-bisphosphate + 2-O-sulfo-α,α-trehalose

Glossary: 2-O-sulfo-α,α-trehalose = trehalose 2-sulfate = α-D-glucopyranosyl 2-O-sulfo-α-D-glucopyranoside

Other name(s): Stf0 sulfotransferase

Systematic name: 3'-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfotransferase

Comments: The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.

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

References:

1. Mougous, J.D., Petzold, C.J., Senaratne, R.H., Lee, D.H., Akey, D.L., Lin, F.L., Munchel, S.E., Pratt, M.R., Riley, L.W., Leary, J.A., Berger, J.M. and Bertozzi, C.R. Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 11 (2004) 721-729. [PMID: 15258569]

2. Pi, N., Hoang, M.B., Gao, H., Mougous, J.D., Bertozzi, C.R. and Leary, J.A. Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry. Anal. Biochem. 341 (2005) 94-104. [PMID: 15866533]

[EC 2.8.2.37 created 2014]


Continued with EC 2.8.3 to EC 2.9.1
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