The Enzyme Database

Your query returned 7 entries.    printer_iconPrintable version



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 2.8.2.33     
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
Other name(s): GalNAc4S-6ST; CHST15 (gene name); 3′-phosphoadenylyl-sulfate:[dermatan]-4-O-sulfo-N-acetyl-D-galactosamine 6-O-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[dermatan]-4-O-sulfo-N-acetyl-D-galactosamine 6-O-sulfonotransferase
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. [DOI] [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. [DOI] [PMID: 11572857]
[EC 2.8.2.33 created 2005, modified 2010]
 
 
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
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, KEGG, MetaCyc, 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]
[EC 3.1.6.4 created 1961]
 
 
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, 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]
[EC 3.1.6.12 created 1984]
 
 
EC 4.2.2.5     
Accepted name: chondroitin AC lyase
Reaction: Eliminative degradation of polysaccharides containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucuronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups
Glossary: chondroitin sulfate A = chondroitin 4-sulfate
chondroitin sulfate C = chondroitin 6-sulfate
For the nomenclature of glycoproteins, glycopeptides and peptidoglycans, click here
Other name(s): chondroitinase (ambiguous); chondroitin sulfate lyase; chondroitin AC eliminase; chondroitinase AC; ChnAC
Systematic name: chondroitin AC lyase
Comments: Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(β1-3)GalNAc(β1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(α1-3)GalNAc(β1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9047-57-8
References:
1.  Nakada, H.I. and Wolfe, J.B. Studies on the enzyme chondroitinase: product structure and ion effects. Arch. Biochem. Biophys. 94 (1961) 244–251. [DOI] [PMID: 13727579]
2.  Pojasek, K., Shriver, Z., Kiley, P., Venkataraman, G. and Sasisekharan, R. Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum. Biochem. Biophys. Res. Commun. 286 (2001) 343–351. [DOI] [PMID: 11500043]
3.  Fethiere, J., Shilton, B.H., Li, Y., Allaire, M., Laliberte, M., Eggimann, B. and Cygler, M. Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 279–280. [PMID: 9761894]
4.  Huckerby, T.N., Nieduszynski, I.A., Giannopoulos, M., Weeks, S.D., Sadler, I.H. and Lauder, R.M. Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides. FEBS J. 272 (2005) 6276–6286. [DOI] [PMID: 16336265]
[EC 4.2.2.5 created 1972 (EC 4.2.99.6 created 1965, part incorporated 1976)]
 
 
EC 4.2.2.20     
Accepted name: chondroitin-sulfate-ABC endolyase
Reaction: Endolytic cleavage of (1→4)-β-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Δ4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Δ4-unsaturated tetra- and disaccharides
For diagram of reaction click here
Glossary: chondroitin sulfate A = chondroitin 4-sulfate
chondroitin sulfate B = dermatan sulfate
chondroitin sulfate C = chondroitin 6-sulfate
For the nomenclature of glycoproteins, glycopeptides and peptidoglycans, click here
Other name(s): chondroitinase (ambiguous); chondroitin ABC eliminase (ambiguous); chondroitinase ABC (ambiguous); chondroitin ABC lyase (ambiguous); chondroitin sulfate ABC lyase (ambiguous); ChS ABC lyase (ambiguous); chondroitin sulfate ABC endoeliminase; chondroitin sulfate ABC endolyase; ChS ABC lyase I
Systematic name: chondroitin-sulfate-ABC endolyase
Comments: This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(β1-3)GalNAc(β1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(α1-3)GalNAc(β1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5]. The related enzyme EC 4.2.2.21, chondroitin-sulfate-ABC exolyase, has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20 [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-13-9
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]
2.  Saito, H., Yamagata, T. and Suzuki, S. Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates. J. Biol. Chem. 243 (1968) 1536–1542. [PMID: 4231029]
3.  Suzuki, S., Saito, H., Yamagata, T., Anno, K., Seno, N., Kawai, Y. and Furuhashi, T. Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion. J. Biol. Chem. 243 (1968) 1543–1550. [PMID: 5647269]
4.  Hamai, A., Hashimoto, N., Mochizuki, H., Kato, F., Makiguchi, Y., Horie, K. and Suzuki, S. Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides. J. Biol. Chem. 272 (1997) 9123–9130. [DOI] [PMID: 9083041]
5.  Huckerby, T.N., Nieduszynski, I.A., Giannopoulos, M., Weeks, S.D., Sadler, I.H. and Lauder, R.M. Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides. FEBS J. 272 (2005) 6276–6286. [DOI] [PMID: 16336265]
[EC 4.2.2.20 created 2006 (EC 4.2.2.4 created 1972, part-incorporated 2006 (EC 4.2.99.6 created 1965, part incorporated 1976))]
 
 
EC 4.2.2.21     
Accepted name: chondroitin-sulfate-ABC exolyase
Reaction: Exolytic removal of Δ4-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
For diagram of reaction click here
Glossary: chondroitin sulfate A = chondroitin 4-sulfate
chondroitin sulfate B = dermatan sulfate
chondroitin sulfate C = chondroitin 6-sulfate
For the nomenclature of glycoproteins, glycopeptides and peptidoglycans, click here
Other name(s): chondroitinase (ambiguous); chondroitin ABC eliminase (ambiguous); chondroitinase ABC (ambiguous); chondroitin ABC lyase (ambiguous); chondroitin sulfate ABC lyase (ambiguous); ChS ABC lyase (ambiguous); chondroitin sulfate ABC exoeliminase; chondroitin sulfate ABC exolyase; ChS ABC lyase II
Systematic name: chondroitin-sulfate-ABC exolyase
Comments: This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. The related enzyme EC 4.2.2.20, chondroitin-sulfate-ABC endolyase, has the same substrate specificity but produces a mixture of oligosaccharides of different sizes that are ultimately degraded to tetra- and disaccharides [4]. Both enzymes act by the removal of a relatively acidic C-5 proton of the uronic acid followed by the elimination of a 4-linked hexosamine, resulting in the formation of an unsaturated C4C5 bond on the hexuronic acid moiety of the products [4,6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000607-06-6
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]
2.  Saito, H., Yamagata, T. and Suzuki, S. Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates. J. Biol. Chem. 243 (1968) 1536–1542. [PMID: 4231029]
3.  Suzuki, S., Saito, H., Yamagata, T., Anno, K., Seno, N., Kawai, Y. and Furuhashi, T. Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion. J. Biol. Chem. 243 (1968) 1543–1550. [PMID: 5647269]
4.  Hamai, A., Hashimoto, N., Mochizuki, H., Kato, F., Makiguchi, Y., Horie, K. and Suzuki, S. Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides. J. Biol. Chem. 272 (1997) 9123–9130. [DOI] [PMID: 9083041]
5.  Huckerby, T.N., Nieduszynski, I.A., Giannopoulos, M., Weeks, S.D., Sadler, I.H. and Lauder, R.M. Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides. FEBS J. 272 (2005) 6276–6286. [DOI] [PMID: 16336265]
6.  Zhang, Z., Park, Y., Kemp, M.M., Zhao, W., Im, A.R., Shaya, D., Cygler, M., Kim, Y.S. and Linhardt, R.J. Liquid chromatography-mass spectrometry to study chondroitin lyase action pattern. Anal. Biochem. 385 (2009) 57–64. [DOI] [PMID: 18992215]
[EC 4.2.2.21 created 2006 (EC 4.2.2.4 created 1972, part-incorporated 2006 (EC 4.2.99.6 created 1965, part incorporated 1976)), modified 2010]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald