The Enzyme Database

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EC 1.8.4.8     
Accepted name: phosphoadenylyl-sulfate reductase (thioredoxin)
Reaction: adenosine 3′,5′-bisphosphate + sulfite + thioredoxin disulfide = 3′-phosphoadenylyl sulfate + thioredoxin
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): PAPS reductase, thioredoxin-dependent; PAPS reductase; thioredoxin:adenosine 3′-phosphate 5′-phosphosulfate reductase; 3′-phosphoadenylylsulfate reductase; thioredoxin:3′-phospho-adenylylsulfate reductase; phosphoadenosine-phosphosulfate reductase; adenosine 3′,5′-bisphosphate,sulfite:oxidized-thioredoxin oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming)
Systematic name: adenosine 3′,5′-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming)
Comments: Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-63-7
References:
1.  Berendt, U., Haverkamp, T., Prior, A., Schwenn, J.D. Reaction mechanism of thioredoxin: 3′-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 (1995) 347–356. [DOI] [PMID: 7588765]
[EC 1.8.4.8 created 1999 as EC 1.8.99.4, transferred 2000 to EC 1.8.4.8]
 
 
EC 2.7.1.25     
Accepted name: adenylyl-sulfate kinase
Reaction: ATP + adenylyl sulfate = ADP + 3′-phosphoadenylyl sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): adenylylsulfate kinase (phosphorylating); 5′-phosphoadenosine sulfate kinase; adenosine 5′-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5′-phosphosulfate-3′-phosphokinase; APS kinase
Systematic name: ATP:adenylyl-sulfate 3′-phosphotransferase
Comments: The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5′-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-38-8
References:
1.  Bandurski, R.S., Wilson, L.G., Squires, C.L. The mechanism of "active sulfate" formation. J. Am. Chem. Soc. 78 (1956) 6408–6409.
2.  Robbins, P.W., Lipmann, F. Isolation and identification of active sulfate. J. Biol. Chem. 229 (1957) 837–851. [PMID: 13502346]
3.  Venkatachalam, K.V., Akita, H., Strott, C. Molecular cloning, expression and characterization of human bifunctional 3′-phosphoadenosine-5′-phosphosulfate synthase and its functional domains. J. Biol. Chem. 273 (1998) 19311–19320. [DOI] [PMID: 9668121]
[EC 2.7.1.25 created 1961, modified 1999]
 
 
EC 2.8.2.1     
Accepted name: aryl sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + a phenol = adenosine 3′,5′-bisphosphate + an aryl sulfate
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
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; 3′-phosphoadenylyl-sulfate:phenol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:phenol sulfonotransferase
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. [DOI] [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; 3′-phosphoadenylyl-sulfate:alcohol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:alcohol sulfonotransferase
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. [DOI] [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; 3′-phosphoadenylyl-sulfate:amine N-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:amine N-sulfonotransferase
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. [PMID: 14439731]
[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 name(s): 3′-phosphoadenylyl sulfate-estrone 3-sulfotransferase; estrogen sulfotransferase; estrogen sulphotransferase; oestrogen sulphotransferase; 3′-phosphoadenylylsulfate:oestrone sulfotransferase; 3′-phosphoadenylyl-sulfate:estrone 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:estrone 3-sulfonotransferase
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. [DOI] [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. [PMID: 903358]
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. Biochim. Biophys. Acta 370 (1974) 160–188. [DOI] [PMID: 4473218]
[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 of chondroitin biosynthesis (later stages), click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): chondroitin sulfotransferase; 3′-phosphoadenylyl-sulfate:chondroitin 4′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:chondroitin 4′-sulfonotransferase
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. [DOI] [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. [DOI] [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. [PMID: 13835879]
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. [PMID: 13835880]
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. [PMID: 13835881]
[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 name(s): choline sulphokinase; 3′-phosphoadenylyl-sulfate:choline sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:choline sulfonotransferase
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. [PMID: 14202240]
[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 name(s): uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase; uridine diphospho-N-acetylgalactosamine 4-sulfate sulfotransferase; 3′-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate 6-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate 6-sulfonotransferase
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 name(s): 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; 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfonotransferase
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. [DOI] [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 name(s): aryl sulfotransferase IV; L-tyrosine methyl ester sulfotransferase; 3′-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfonotransferase
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, PDB, 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) 11123–11127. [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. [DOI] [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); 3′-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:Renilla luciferin sulfonotransferase
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 name(s): GSase; 3′-phosphoadenosine-5′-phosphosulfate-cerebroside sulfotransferase; galactocerebroside sulfotransferase; galactolipid sulfotransferase; glycolipid sulfotransferase; glycosphingolipid sulfotransferase; 3′-phosphoadenylyl-sulfate:galactosylceramide 3′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:galactosylceramide 3′-sulfonotransferase
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. [DOI] [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 2.8.2.13     
Accepted name: psychosine sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + galactosylsphingosine = adenosine 3′,5′-bisphosphate + psychosine sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): PAPS:psychosine sulphotransferase; 3′-phosphoadenosine 5′-phosphosulfate-psychosine sulphotransferase; 3′-phosphoadenylyl-sulfate:galactosylsphingosine sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:galactosylsphingosine sulfonotransferase
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. [DOI] [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 of reaction, click here and for diagram of cholic acid conjugates biosynthesis, click here
Glossary: glycolithocholate 3-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; 3′-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:glycolithocholate sulfonotransferase
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. [DOI] [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. [DOI] [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 name(s): steroid alcohol sulfotransferase; 3′-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:phenolic-steroid sulfonotransferase
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. [DOI] [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 name(s): phosphoadenylylsulfate-thiol sulfotransferase; PAPS sulfotransferase; adenosine 3′-phosphate 5′-sulphatophosphate sulfotransferase; 3′-phosphoadenylyl-sulfate:thiol S-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:thiol S-sulfonotransferase
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. [PMID: 24424637]
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 of chondroitin biosynthesis (later stages), click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): chondroitin 6-O-sulfotransferase; 3′-phosphoadenosine 5′-phosphosulfate (PAPS):chondroitin sulfate sulfotransferase; terminal 6-sulfotransferase; 3′-phosphoadenylyl-sulfate:chondroitin 6′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:chondroitin 6′-sulfonotransferase
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. [DOI] [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; 3′-phosphoadenylyl-sulfate:cortisol 21-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:cortisol 21-sulfonotransferase
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. [DOI] [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. [DOI] [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 name(s): triglucosylmonoalkylmonoacyl sulfotransferase; 3′-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol 6-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol 6-sulfonotransferase
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; 3′-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:protein-tyrosine O-sulfonotransferase
Comments: The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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 name(s): 3′-phosphoadenylyl keratan sulfotransferase; keratan sulfate sulfotransferase; 3′-phosphoadenylylsulfate:keratan sulfotransferase; 3′-phosphoadenylyl-sulfate:keratan 6′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:keratan 6′-sulfonotransferase
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 name(s): arylsulfate-phenol sulfotransferase; arylsulfotransferase (ambiguous); ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name); aryl-sulfate:phenol sulfotransferase
Systematic name: aryl-sulfate:phenol sulfonotransferase
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. [DOI] [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
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); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11375390]
[EC 2.8.2.23 created 1992, modified 2001]
 
 
EC 2.8.2.24     
Accepted name: aromatic desulfoglucosinolate sulfotransferase
Reaction: (1) 3′-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3′,5′-bisphosphate + glucotropeolin
(2) 3′-phosphoadenylyl sulfate + indolylmethyl-desulfoglucosinolate = adenosine 3′,5′-bisphosphate + glucobrassicin
For diagram of glucotropeolin biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): desulfoglucosinolate sulfotransferase (ambiguous); PAPS-desulfoglucosinolate sulfotransferase (ambiguous); 3′-phosphoadenosine-5′-phosphosulfate:desulfoglucosinolate sulfotransferase (ambiguous); 3′-phosphoadenylyl-sulfate:aromatic desulfoglucosinolate sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:aromatic desulfoglucosinolate sulfonotransferase
Comments: This enzyme, characterized from cruciferous plants, catalyses the last step in the biosynthesis of tryptophan- and phenylalanine-derived glucosinolates. cf. EC 2.8.2.38, aliphatic desulfoglucosinolate sulfotransferase.
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. [DOI] [PMID: 2524977]
2.  Klein, M., Reichelt, M., Gershenzon, J. and Papenbrock, J. The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed. FEBS J. 273 (2006) 122–136. [DOI] [PMID: 16367753]
3.  Klein, M. and Papenbrock, J. Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana. Physiol. Plant. 135 (2009) 140–149. [DOI] [PMID: 19077143]
[EC 2.8.2.24 created 1992, modified 2017]
 
 
EC 2.8.2.25     
Accepted name: flavonol 3-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + quercetin = adenosine 3′,5′-bisphosphate + quercetin 3-sulfate
For diagram of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): 3′-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin 3-sulfonotransferase
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. [PMID: 16666908]
[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 of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 3′-sulfotransferase; 3′-Sulfotransferase; PAPS:flavonol 3-sulfate 3′-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 3′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 3′-sulfonotransferase
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. [PMID: 16666908]
[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 of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 4′-sulfotransferase; PAPS:flavonol 3-sulfate 4′-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 4′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 4′-sulfonotransferase
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. [PMID: 16666908]
[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 of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 7-sulfotransferase; 7-sulfotransferase; PAPS:flavonol 3,3′/3,4′-disulfate 7-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3,3′-bissulfate 7-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3,3′-bissulfate 7-sulfonotransferase
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); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
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
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. [DOI] [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. [DOI] [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): 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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 of reaction, click here
Glossary: petromyzonol = 5α-cholan-3α,7α,12α,24-tetrol
3′-phosphoadenylyl sulfate = PAPS
Other name(s): PZ-SULT; 3′-phosphoadenylyl-sulfate:5α-cholan-3α,7α,12α,24-tetrol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:5α-cholan-3α,7α,12α,24-tetrol sulfonotransferase
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
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. [DOI] [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 of reaction, 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 name(s): 3′-phosphoadenylyl sulfate:5β-scymnol sulfotransferase
Systematic name: 3′-phosphoadenylyl sulfate:5β-scymnol sulfonotransferase
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. 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. 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. 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. 121 (1998) 341–348.
[EC 2.8.2.32 created 2005]
 
 
EC 2.8.2.34     
Accepted name: glycochenodeoxycholate sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3′,5′-bisphosphate + glycochenodeoxycholate 7-sulfate
For diagram of reaction, 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; 3′-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfonotransferase
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. [DOI] [PMID: 12543708]
[EC 2.8.2.34 created 2005]
 
 
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; 3′-phosphoadenylyl-sulfate:desulfo-A47934 sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:desulfo-A47934 sulfonotransferase
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
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. [DOI] [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. [DOI] [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; 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfonotransferase
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
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. [DOI] [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. [DOI] [PMID: 15866533]
[EC 2.8.2.37 created 2014]
 
 
EC 2.8.2.38     
Accepted name: aliphatic desulfoglucosinolate sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + an aliphatic desulfoglucosinolate = adenosine 3′,5′-bisphosphate + an aliphatic glucosinolate
Other name(s): SOT17 (gene name); SOT18 (gene name); 3′-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfonotransferase
Comments: The enzyme catalyses the last step in the biosynthesis of aliphatic glucosinolate core structures. cf. EC 2.8.2.24, aromatic desulfoglucosinolate sulfotransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Piotrowski, M., Schemenewitz, A., Lopukhina, A., Muller, A., Janowitz, T., Weiler, E.W. and Oecking, C. Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure. J. Biol. Chem. 279 (2004) 50717–50725. [DOI] [PMID: 15358770]
2.  Klein, M., Reichelt, M., Gershenzon, J. and Papenbrock, J. The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed. FEBS J. 273 (2006) 122–136. [DOI] [PMID: 16367753]
3.  Klein, M. and Papenbrock, J. Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana. Physiol. Plant. 135 (2009) 140–149. [DOI] [PMID: 19077143]
[EC 2.8.2.38 created 2017]
 
 
EC 3.1.3.7     
Accepted name: 3′(2′),5′-bisphosphate nucleotidase
Reaction: adenosine 3′,5′-bisphosphate + H2O = AMP + phosphate
Other name(s): phosphoadenylate 3′-nucleotidase; 3′-phosphoadenylylsulfate 3′-phosphatase; 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase
Systematic name: adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase
Comments: Also acts on 3′-phosphoadenylyl sulfate, and on the corresponding 2′-phosphates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-83-6
References:
1.  Brungraber, E.G. Nucleotides involved in the enzymatic conjugation of phenols with sulfate. J. Biol. Chem. 233 (1958) 472–477. [PMID: 13563523]
2.  Farooqui, A.A. and Balasubramanian, A.S. Enzymatic dephosphorylation 3′-phosphoadenosine 5′-phosphosulfate to adenosine 5′-phosphosulfate in sheep brain. Biochim. Biophys. Acta 198 (1970) 56–65. [DOI] [PMID: 4313079]
3.  Ramaswamy, S.G. and Jakoby, W.B. (2′)3′,5′-Bisphosphate nucleotidase. J. Biol. Chem. 262 (1987) 10044–10047. [PMID: 3038862]
4.  Tsang, M. L.-S. and Schiff, J.A. Properties of enzyme fraction A from Chlorella and copurification of 3′ (2′), 5′-biphosphonucleoside 3′ (2′)-phosphohydrolase, adenosine 5′phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities. Eur. J. Biochem. 65 (1976) 113–121. [DOI] [PMID: 179817]
[EC 3.1.3.7 created 1961]
 
 
EC 3.6.2.2     
Accepted name: phosphoadenylylsulfatase
Reaction: 3′-phosphoadenylyl sulfate + H2O = adenosine 3′,5′-bisphosphate + sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): 3-phosphoadenylyl sulfatase; 3-phosphoadenosine 5-phosphosulfate sulfatase; PAPS sulfatase; 3′-phosphoadenylylsulfate sulfohydrolase
Systematic name: 3′-phosphoadenylyl-sulfate sulfohydrolase
Comments: Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-37-5
References:
1.  Balasubramanian, A.S. and Bachhawat, B.K. Enzymic degradation of active sulphate. Biochim. Biophys. Acta 59 (1962) 389–397. [DOI] [PMID: 13864264]
[EC 3.6.2.2 created 1972]
 
 


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