EC |
3.1.6.1 |
Accepted name: |
arylsulfatase (type I) |
Reaction: |
an aryl sulfate + H2O = a phenol + sulfate |
Other name(s): |
sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; type I sulfatase; arylsulfatase |
Systematic name: |
aryl-sulfate sulfohydrolase |
Comments: |
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, formylglycine-generating enzyme, EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9016-17-5 |
References: |
1. |
Dodgson, K.S., Spencer, B. and Williams, K. Studies on sulphatases. 13. The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metacaligenes. Biochem. J. 64 (1956) 216–221. [PMID: 13363831] |
2. |
Webb, E.C. and Morrow, P.F.W. The activation of an arysulphatase from ox liver by chloride and other anions. Biochem. J. 73 (1959) 7–15. [PMID: 13843260] |
3. |
Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205–235. [PMID: 13744184] |
4. |
Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111–135. [PMID: 13772] |
5. |
Schmidt, B., Selmer, T., Ingendoh, A. and von Figura, K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82 (1995) 271–278. [PMID: 7628016] |
6. |
Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273 (1998) 25560–25564. [DOI] [PMID: 9748219] |
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[EC 3.1.6.1 created 1961, modified 2011, modified 2021] |
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EC |
3.1.6.2 |
Accepted name: |
steryl-sulfatase |
Reaction: |
3β-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3β-hydroxyandrost-5-en-17-one + sulfate |
Other name(s): |
arylsulfatase; steroid sulfatase; sterol sulfatase; dehydroepiandrosterone sulfate sulfatase; arylsulfatase C; steroid 3-sulfatase; steroid sulfate sulfohydrolase; dehydroepiandrosterone sulfatase; pregnenolone sulfatase; phenolic steroid sulfatase; 3-β-hydroxysteroid sulfate sulfatase |
Systematic name: |
steryl-sulfate sulfohydrolase |
Comments: |
Also acts on some related steryl sulfates. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-62-1 |
References: |
1. |
Roy, A.B. The steroid sulphatase of Patella vlugata. Biochim. Biophys. Acta 15 (1954) 300–301. [DOI] [PMID: 13208702] |
2. |
Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205–235. [PMID: 13744184] |
3. |
Stitch, S.R., Halkerston, I.D.K. and Hillman, J. The enzymic hydrolysis of steroid conjugates. 1. Sulphatase and β-glucuronidase activity of molluscan extracts. Biochem. J. 63 (1965) 705–710. [PMID: 13355874] |
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[EC 3.1.6.2 created 1961] |
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EC |
3.1.6.3 |
Accepted name: |
glycosulfatase |
Reaction: |
D-glucose 6-sulfate + H2O = D-glucose + sulfate |
Other name(s): |
glucosulfatase |
Systematic name: |
sugar-sulfate sulfohydrolase |
Comments: |
Also acts on other sulfates of monosaccharides and disaccharides and on adenosine 5′-sulfate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-61-0 |
References: |
1. |
Dodgson, K.S. Glycosulphatase: observations on the activity of partially purified preparations towards the sulphate esters of certain monosaccharides and steroids. Biochem. J. 78 (1961) 324–333. [PMID: 16748876] |
2. |
Egami, F. and Takahaski, N. Syntheses of adenosinesulfuric acids. Bull. Chem. Soc. Jpn. 28 (1955) 666–668. |
3. |
Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205–235. [PMID: 13744184] |
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[EC 3.1.6.3 created 1961] |
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EC |
3.1.6.4 |
Accepted name: |
N-acetylgalactosamine-6-sulfatase |
Reaction: |
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate |
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For diagram of the later stages of chondroitin biosynthesis, click here |
Other name(s): |
chondroitin sulfatase; chondroitinase; galactose-6-sulfate sulfatase; acetylgalactosamine 6-sulfatase; N-acetylgalactosamine-6-sulfate sulfatase; N-acetylgalactosamine 6-sulfatase |
Systematic name: |
N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-60-9 |
References: |
1. |
Epstein, E.H. and Leventhal, M.E. Steroid sulfatase of human leukocytes and epidermis and the diagnosis of recessive X-linked ichthyosis. J. Clin. Invest. 67 (1981) 1257–1262. [DOI] [PMID: 6939689] |
2. |
Glössl, J. and Kresse, H. Impaired degradation of keratan sulphate by Morquio A fibroblasts. Biochem. J. 203 (1982) 335–338. [PMID: 6213226] |
3. |
Lim, C.T. and Horwitz, A.L. Purification and properties of human N-acetylgalactosamine-6-sulfate sulfatase. Biochim. Biophys. Acta 657 (1981) 344–355. [DOI] [PMID: 7213753] |
4. |
Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity. Eur. J. Biochem. 126 (1982) 559–568. [DOI] [PMID: 6814909] |
5. |
Yutaka, T., Okada, S., Kato, T., Inui, K. and Yabuchi, H. Galactose 6-sulfate sulfatase activity in Morquio syndrome. Clin. Chim. Acta 122 (1982) 169–180. [DOI] [PMID: 6809361] |
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[EC 3.1.6.4 created 1961] |
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EC
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3.1.6.5
|
Deleted entry: | sinigrin sulfohydrolase; myrosulfatase |
[EC 3.1.6.5 created 1961, deleted 1964] |
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EC |
3.1.6.6 |
Accepted name: |
choline-sulfatase |
Reaction: |
choline sulfate + H2O = choline + sulfate |
Systematic name: |
choline-sulfate sulfohydrolase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-59-6 |
References: |
1. |
Takebe, I. Isolation and characterization of a new enzyme choline sulfatase. J. Biochem. (Tokyo) 50 (1961) 245–255. [PMID: 13919191] |
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[EC 3.1.6.6 created 1965] |
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EC |
3.1.6.7 |
Accepted name: |
cellulose-polysulfatase |
Reaction: |
Hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin |
Systematic name: |
cellulose-sulfate sulfohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-58-5 |
References: |
1. |
Takahashi, N. and Egami, F. Hydrolysis of polysaccharide sulphate esters by a sulphatase preparation from Charonia lampas. Biochem. J. 80 (1961) 384–386. [PMID: 13774882] |
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[EC 3.1.6.7 created 1965] |
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EC |
3.1.6.8 |
Accepted name: |
cerebroside-sulfatase |
Reaction: |
a cerebroside 3-sulfate + H2O = a cerebroside + sulfate |
Other name(s): |
arylsulfatase A; cerebroside sulfate sulfatase |
Systematic name: |
cerebroside-3-sulfate 3-sulfohydrolase |
Comments: |
Hydrolyses galactose-3-sulfate residues in a number of lipids. Also hydrolyses ascorbate 2-sulfate and many phenol sulfates. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9068-68-2 |
References: |
1. |
Mehl, E. and Jatzkewitz, H. A cerebrosidesulfatase from swine kidney. Hoppe-Seyler's Z. Physiol. Chem. 339 (1964) 260–276. [PMID: 5829234] |
2. |
Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111–135. [PMID: 13772] |
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[EC 3.1.6.8 created 1972] |
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EC |
3.1.6.9 |
Accepted name: |
chondro-4-sulfatase |
Reaction: |
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 4-sulfate + H2O = 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate |
Other name(s): |
chondroitin-4-sulfatase; 4-deoxy-β-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase |
Systematic name: |
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase |
Comments: |
Also acts on the saturated analogue but not on higher oligosaccharides, nor any 6-sulfates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9045-75-4 |
References: |
1. |
Held, V.E. and Buddecke, E. Nachweis, Reinigung und Eigenschaften einer Chondroitin-4-Sulfatase aus der Aorta des Rindes. Hoppe-Seyler's Z. Physiol. Chem. 348 (1967) 1047–1060. [PMID: 5595107] |
2. |
Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111–135. [PMID: 13772] |
3. |
Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S. Purification and properties of bacterial chondroitinases and chondrosulfatases. J. Biol. Chem. 243 (1968) 1523–1535. [PMID: 5647268] |
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[EC 3.1.6.9 created 1972] |
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EC |
3.1.6.10 |
Accepted name: |
chondro-6-sulfatase |
Reaction: |
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 6-sulfate + H2O = 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate |
Other name(s): |
4-deoxy-β-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase |
Systematic name: |
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase |
Comments: |
Also acts on the saturated analogue and N-acetyl-D-galactosamine 4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9045-76-5 |
References: |
1. |
Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S. Purification and properties of bacterial chondroitinases and chondrosulfatases. J. Biol. Chem. 243 (1968) 1523–1535. [PMID: 5647268] |
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[EC 3.1.6.10 created 1972] |
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EC |
3.1.6.11 |
Accepted name: |
disulfoglucosamine-6-sulfatase |
Reaction: |
2-N,6-O-disulfo-D-glucosamine + H2O = 2-N-sulfo-D-glucosamine + sulfate |
Other name(s): |
N-sulfoglucosamine-6-sulfatase; 6,N-disulfoglucosamine 6-O-sulfohydrolase; N,6-O-disulfo-D-glucosamine 6-sulfohydrolase |
Systematic name: |
2-N,6-O-disulfo-D-glucosamine 6-sulfohydrolase |
Comments: |
May be identical with EC 3.1.6.14 N-acetylglucosamine-6-sulfatase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37288-32-7 |
References: |
1. |
Dietrich, C.P. Enzymic degradation of heparin. A sulphamidase and a sulphoesterase from Flavobacterium heparinum. Biochem. J. 111 (1969) 91–95. [PMID: 5775690] |
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[EC 3.1.6.11 created 1972, modified 1989] |
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EC |
3.1.6.12 |
Accepted name: |
N-acetylgalactosamine-4-sulfatase |
Reaction: |
Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate |
|
For diagram of the later stages of chondroitin biosynthesis, click here |
Other name(s): |
chondroitinsulfatase; chondroitinase; arylsulfatase B; acetylgalactosamine 4-sulfatase; N-acetylgalactosamine 4-sulfate sulfohydrolase |
Systematic name: |
N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase |
Comments: |
Acts also on N-acetylglucosamine 4-sulfate. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 55354-43-3 |
References: |
1. |
Farooqui, A.A. The desulphation of hexosamine sulphates by arylsulphatase B. Experientia 32 (1976) 1242–1244. [PMID: 976430] |
2. |
Gorham, S.D. and Cantz, M. Arylsulphatase B, an exo-sulphatase for chondroitin 4-sulphate tetrasaccharide. Hoppe-Seyler's Z. Physiol. Chem. 359 (1978) 1811–1814. [PMID: 738706] |
3. |
Tsuji, M., Nakanishi, Y., Habuchi, H., Ishihara, K. and Suzuki, S. The common identity of UDP-N-acetylgalactosamine 4-sulfatase, nitrocatechol sulfatase (arylsulfatase), and chondroitin 4-sulfatase. Biochim. Biophys. Acta 612 (1980) 373–383. [DOI] [PMID: 7370276] |
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[EC 3.1.6.12 created 1984] |
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EC |
3.1.6.13 |
Accepted name: |
iduronate-2-sulfatase |
Reaction: |
Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin |
Other name(s): |
chondroitinsulfatase; idurono-2-sulfatase; iduronide-2-sulfate sulfatase; L-iduronosulfatase; L-idurono sulfate sulfatase; iduronate sulfatase; sulfo-L-iduronate sulfatase; L-iduronate 2-sulfate sulfatase; sulfoiduronate sulfohydrolase; 2-sulfo-L-iduronate 2-sulfatase; iduronate-2-sulfate sulfatase; iduronate sulfate sulfatase |
Systematic name: |
L-iduronate-2-sulfate 2-sulfohydrolase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 50936-59-9 |
References: |
1. |
Archer, I.M., Harper, P.S. and Wusteman, F.S. Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids. Biochim. Biophys. Acta 708 (1982) 134–140. [DOI] [PMID: 6816283] |
2. |
Bach, J., Eisenberg, F., Cantz, M. and Neufeld, E.C. The defect in the Hunter syndrome: deficiency of sulfoiduronate sulfatase. Proc. Natl. Acad. Sci. USA 70 (1973) 2134–2138. [DOI] [PMID: 4269173] |
3. |
DiNatale, P. and Ronsivalle, L. Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta. Biochim. Biophys. Acta 661 (1981) 106–111. [DOI] [PMID: 6945876] |
4. |
Yutaka, T., Fluharty, A.L., Stevens, R.L. and Kihara, H. Purification and some properties of human liver iduronate sulfatase. J. Biochem. (Tokyo) 91 (1982) 433–441. [PMID: 6950934] |
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[EC 3.1.6.13 created 1984] |
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EC |
3.1.6.14 |
Accepted name: |
N-acetylglucosamine-6-sulfatase |
Reaction: |
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate |
Other name(s): |
chondroitinsulfatase; O,N-disulfate O-sulfohydrolase; acetylglucosamine 6-sulfatase; N-acetylglucosamine 6-sulfate sulfatase; acetylglucosamine 6-sulfatase; 2-acetamido-2-deoxy-D-glucose 6-sulfate sulfatase |
Systematic name: |
N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase |
Comments: |
May be identical with EC 3.1.6.11 disulfoglucosamine-6-sulfatase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 65666-34-4 |
References: |
1. |
Basner, R., Kresse, H. and von Figura, K. N-Acetylglucosamine-6-sulfate sulfatase from human urine. J. Biol. Chem. 254 (1979) 1151–1158. [PMID: 762121] |
2. |
Kresse, H., Fuchs, W., Glössl, J., Holtfrerich, D. and Gilberg, W. Liberation of N-acetylglucosamine-6-sulfate by human β-N-acetylhexosaminidase A. J. Biol. Chem. 256 (1981) 12926–12932. [PMID: 6458607] |
3. |
Weissmann, B., Chao, H. and Chow, P. A glucosamine O,N-disulfate O-sulfohydrolase with a probable role in mammalian catabolism of heparan sulfate. Biochem. Biophys. Res. Commun. 97 (1980) 827–833. [DOI] [PMID: 6451222] |
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[EC 3.1.6.14 created 1984] |
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EC |
3.1.6.15 |
Accepted name: |
N-sulfoglucosamine-3-sulfatase |
Reaction: |
Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin |
Other name(s): |
chondroitinsulfatase |
Systematic name: |
N-sulfo-3-sulfoglucosamine 3-sulfohydrolase |
Comments: |
The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
References: |
1. |
Bruce, J.S., McLean, M.W., Long, W.F. and Williamson, F.B. Flavobacterium heparinum 3-O-sulphatase for N-substituted glucosamine 3-O-sulphate. Eur. J. Biochem. 148 (1985) 359–365. [DOI] [PMID: 3987694] |
2. |
Leder, I.G. A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-α-D-glucopyranoside 3-sulfate. Biochem. Biophys. Res. Commun. 94 (1980) 1183–1189. [DOI] [PMID: 7396957] |
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[EC 3.1.6.15 created 1984, modified 1989] |
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EC |
3.1.6.16 |
Accepted name: |
monomethyl-sulfatase |
Reaction: |
monomethyl sulfate + H2O = methanol + sulfate |
Systematic name: |
monomethyl-sulfate sulfohydrolase |
Comments: |
Highly specific; does not act on monoethyl sulfate, monoisopropyl sulfate or monododecyl sulfate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ghisalba, O. and Küenzi, M. Biodegradation and utilization of monomethyl sulfate by specialized methylotrophs. Experientia 39 (1983) 1257–1263. [PMID: 6641899] |
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[EC 3.1.6.16 created 1989] |
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EC |
3.1.6.17 |
Accepted name: |
D-lactate-2-sulfatase |
Reaction: |
(R)-2-O-sulfolactate + H2O = (R)-lactate + sulfate |
Other name(s): |
(S)-2-O-sulfolactate 2-sulfohydrolase (incorrect stereochemistry) |
Systematic name: |
(R)-2-O-sulfolactate 2-sulfohydrolase |
Comments: |
Highly specific. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93586-05-1 |
References: |
1. |
Crescenzi, A.M.V., Dodgson, K.S. and White, G.F. Purification and some properties of the D-lactate-2-sulphatase of Pseudomonas syringae GG. Biochem. J. 223 (1984) 487–494. [PMID: 6497859] |
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[EC 3.1.6.17 created 1989] |
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EC |
3.1.6.18 |
Accepted name: |
glucuronate-2-sulfatase |
Reaction: |
Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate |
Other name(s): |
glucurono-2-sulfatase |
Systematic name: |
polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase |
Comments: |
Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13 iduronate-2-sulfatase) |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 98597-45-6 |
References: |
1. |
Shaklee, P.N., Glaser, J.H. and Conrad, H.E. A sulfatase specific for glucuronic acid 2-sulfate residues in glycosaminoglycans. J. Biol. Chem. 260 (1985) 9146–9149. [PMID: 4019466] |
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[EC 3.1.6.18 created 1989] |
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EC |
3.1.6.19 |
Accepted name: |
(R)-specific secondary-alkylsulfatase (type III) |
Reaction: |
an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate |
Other name(s): |
S3 secondary alkylsulphohydrolase; Pisa1; secondary alkylsulphohydrolase; (R)-specific sec-alkylsulfatase; sec-alkylsulfatase; (R)-specific secondary-alkylsulfatase; type III (R)-specific secondary-alkylsulfatase |
Systematic name: |
(R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol-forming] |
Comments: |
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Pogorevc, M. and Faber, K. Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541. Appl. Environ. Microbiol. 69 (2003) 2810–2815. [DOI] [PMID: 12732552] |
2. |
Wallner, S.R., Nestl, B.M. and Faber, K. Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639. Org. Lett. 6 (2004) 5009–5010. [DOI] [PMID: 15606122] |
3. |
Knaus, T., Schober, M., Kepplinger, B., Faccinelli, M., Pitzer, J., Faber, K., Macheroux, P. and Wagner, U. Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates. FEBS J. 279 (2012) 4374–4384. [DOI] [PMID: 23061549] |
4. |
Schober, M., Knaus, T., Toesch, M., Macheroux, P., Wagner, U. and Faber, K. The substrate spectrum of the inverting sec-alkylsulfatase Pisa1. Adv. Synth. Catal. 354 (2012) 1737–1742. [DOI] |
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[EC 3.1.6.19 created 2013, modified 2021] |
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EC |
3.1.6.20 |
Accepted name: |
S-sulfosulfanyl-L-cysteine sulfohydrolase |
Reaction: |
(1) [SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O = [SoxY protein]-S-sulfanyl-L-cysteine + sulfate (2) [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O = [SoxY protein]-S-disulfanyl-L-cysteine + sulfate |
Other name(s): |
SoxB |
Systematic name: |
[SoxY protein]-S-sulfosulfanyl-L-cysteine sulfohydrolase |
Comments: |
Contains Mn2+. The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway. In both cases the enzyme hydrolyses a sulfonate moiety that is bound (either directly or via a sulfane) to a cysteine residue of a SoxY protein, releasing sulfate. The enzyme from Paracoccus pantotrophus contains a pyroglutamate (cycloglutamate) at its N-terminus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Quentmeier, A. and Friedrich, C.G. The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17. FEBS Lett. 503 (2001) 168–172. [PMID: 11513876] |
2. |
Friedrich, C.G., Rother, D., Bardischewsky, F., Quentmeier, A. and Fischer, J. Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism. Appl. Environ. Microbiol. 67 (2001) 2873–2882. [DOI] [PMID: 11425697] |
3. |
Quentmeier, A., Hellwig, P., Bardischewsky, F., Grelle, G., Kraft, R. and Friedrich, C.G. Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein. Biochem. Biophys. Res. Commun. 312 (2003) 1011–1018. [PMID: 14651972] |
4. |
Epel, B., Schafer, K.O., Quentmeier, A., Friedrich, C. and Lubitz, W. Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus. J. Biol. Inorg. Chem. 10 (2005) 636–642. [PMID: 16133204] |
5. |
Hensen, D., Sperling, D., Truper, H.G., Brune, D.C. and Dahl, C. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62 (2006) 794–810. [PMID: 16995898] |
6. |
Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12:e0173395 (2017). [DOI] [PMID: 28257465] |
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[EC 3.1.6.20 created 2018] |
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EC |
3.1.6.21 |
Accepted name: |
linear primary-alkylsulfatase |
Reaction: |
a primary alkyl sulfate ester + H2O = an alcohol + sulfate |
Other name(s): |
sdsA1 (gene name); yjcS (gene name); type III linear primary-alkylsulfatase |
Systematic name: |
primary alkyl sulfate ester sulfohydrolase |
Comments: |
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. It is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 3.1.6.22, branched primary-alkylsulfatase, and EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hagelueken, G., Adams, T.M., Wiehlmann, L., Widow, U., Kolmar, H., Tummler, B., Heinz, D.W. and Schubert, W.D. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proc. Natl. Acad. Sci. USA 103 (2006) 7631–7636. [DOI] [PMID: 16684886] |
2. |
Long, M., Ruan, L., Li, F., Yu, Z. and Xu, X. Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP). Extremophiles 15 (2011) 293–301. [DOI] [PMID: 21318560] |
3. |
Liang, Y., Gao, Z., Dong, Y. and Liu, Q. Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase. Protein Sci. 23 (2014) 1442–1450. [DOI] [PMID: 25066955] |
4. |
Sun, L., Chen, P., Su, Y., Cai, Z., Ruan, L., Xu, X. and Wu, Y. Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9. Biosci Rep 37 (2017) . [DOI] [PMID: 28442601] |
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[EC 3.1.6.21 created 2021] |
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EC |
3.1.6.22 |
Accepted name: |
branched primary-alkylsulfatase |
Reaction: |
2-butyloctyl sulfate + H2O = 2-butyloctan-1-ol + sulfate |
Other name(s): |
DP1 (gene name); type III branched primary-alkylsulfatase |
Systematic name: |
branched primary-alkyl sulfate ester sulfohydrolase |
Comments: |
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III family. The enzyme, characterized from a Pseudomonas strain, is specific for branched primary-alkyl sulfate esters and does not act on linear substrates such as dodecyl sulfate. cf. EC 3.1.6.1, arylsulfatase (type I), EC 1.14.11.77, alkyl sulfatase, EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III) and EC 3.1.6.21, linear primary-alkylsulfatase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ellis, A.J., Hales, S.G., Ur-Rehman, N.G. and White, G.F. Novel alkylsulfatases required for biodegradation of the branched primary alkyl sulfate surfactant 2-butyloctyl sulfate. Appl. Environ. Microbiol. 68 (2002) 31–36. [PMID: 11772605] |
2. |
Toesch, M., Schober, M. and Faber, K. Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities. Appl. Microbiol. Biotechnol. 98 (2014) 1485–1496. [DOI] [PMID: 24352732] |
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[EC 3.1.6.22 created 2021] |
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