Continued from EC 4.2.1.51 to EC 4.2.1.183
Accepted name: hyaluronate lyase
Reaction: Cleaves hyaluronate chains at a β-D-GlcNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Other name(s): hyaluronidase [but cf. EC 3.2.1.35 (hyalurononglucosaminidase) and EC 3.2.1.36 (hyaluronoglucuronidase)]; glucuronoglycosaminoglycan lyase; spreading factor; mucinase
Systematic name: hyaluronate lyase
Comments: The enzyme catalyses the degradation of hyaluronan by a β-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37259-53-3
References:
1. Linker, A., Hoffman, P., Meyer, K., Sampson, P. and Korn, E.D. The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to α-keto acid by bacterial enzymes. J. Biol. Chem. 235 (1960) 3061.
2. Meyer, K. and Rapport, M.M. Hyaluronidases. Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199-236.
3. Moran, F., Nasuno, S. and Starr, M.P. Extracellular and intracellular polygalacturonic acid trans-eliminases of Erwinia carotovora. Arch. Biochem. Biophys. 123 (1968) 298-306. [PMID: 5642600]
Accepted name: pectate lyase
Reaction: Eliminative cleavage of (1→4)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends
For diagram click here.
Other name(s): polygalacturonic transeliminase; pectic acid transeliminase; polygalacturonate lyase; endopectin methyltranseliminase; pectate transeliminase; endogalacturonate transeliminase; pectic acid lyase; pectic lyase; α-1,4-D-endopolygalacturonic acid lyase; PGA lyase; PPase-N; endo-α-1,4-polygalacturonic acid lyase; polygalacturonic acid lyase; pectin trans-eliminase; Polygalacturonic acid trans-eliminase
Systematic name: (1→4)-α-D-galacturonan lyase
Comments: Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9015-75-2
References:
1. Albersheim, P. and Killias, U. Studies relating to the purification and properties of pectin transeliminase. Arch. Biochem. Biophys. 97 (1962) 107-115.
2. Edstrom, R.D. and Phaff, H.J. Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus. J. Biol. Chem. 239 (1964) 2403-2408.
3. Edstrom, R.D. and Phaff, H.J. Eliminative cleavage of pectin and of oligogalacturonide methyl esters by pectin trans-eliminase. J. Biol. Chem. 239 (1964) 2409-2415.
4. Nagel, C.W. and Vaughn, R.H. The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa. Arch. Biochem. Biophys. 94 (1961) 328.
5. Nasuno, S. and Starr, M.P. Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J. 104 (1967) 178-185. [PMID: 6035509]
6. Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5 (1997) 677-689. [PMID: 9195887]
Accepted name: mannuronate-specific alginate lyase
Reaction: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at their reducing end.
Other name(s): alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly(β-D-1,4-mannuronide) lyase; poly(β-D-mannuronate) lyase; aly (gene name) (ambiguous); poly[(1→4)-β-D-mannuronide] lyase
Systematic name: alginate β-D-mannuronate—uronate lyase
Comments: The enzyme catalyses the degradation of alginate by a β-elimination reaction. It cleaves the (1→4) bond between β-D-mannuronate and either α-L-guluronate or β-D-mannuronate, generating oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products. cf. EC 4.2.2.11, guluronate-specific alginate lyase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-15-1
References:
1. Davidson, I.W., Lawson, C.J. and Sutherland, I.W. An alginate lysate from Azotobacter vinelandii phage. J. Gen. Microbiol. 98 (1977) 223-229. [PMID: 13144]
2. Nakada, H.I. and Sweeny, P.C. Alginic acid degradation by eliminases from abalone hepatopancreas. J. Biol. Chem. 242 (1967) 845-851. [PMID: 6020438]
3. Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid. J. Biol. Chem. 237 (1962) 309-316. [PMID: 14488584]
[EC 4.2.2.4 Transferred entry: chondroitin ABC lyase. Now known to comprise two enzymes: EC 4.2.2.20, chondroitin-sulfate-ABC endolyase and EC 4.2.2.21, chondroitin-sulfate-ABC exolyase. (EC 4.2.2.4 created 1972 (EC 4.2.99.6 created 1965, part incorporated 1976), deleted 2006)]
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; chondroitin AC lyase; 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. [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. [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. [PMID: 16336265]
Accepted name: oligogalacturonide lyase
Reaction: 4-(4-deoxy-α-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
Other name(s): oligogalacturonate lyase; unsaturated oligogalacturonate transeliminase; OGTE
Systematic name: oligogalacturonide lyase
Comments: Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-33-8
References:
1. Moran, F., Nasuno, S. and Starr, M.P. Oligogalacturonide trans-eliminase of Erwinia carotovora. Arch. Biochem. Biophys. 125 (1968) 734-741. [PMID: 5671040]
Accepted name: heparin lyase
Reaction: Eliminative cleavage of polysaccharides containing (1→4)-linked D-glucuronate or L-iduronate residues and (1→4)-α-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-α-D-gluc-4-enuronosyl groups at their non-reducing ends
Other name(s): heparin eliminase; heparinase
Systematic name: heparin lyase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-39-2
References:
1. Hovingh, P. and Linker, A. The enzymatic degradation of heparin and heparitin sulfate. 3. Purification of a heparitinase and a heparinase from flavobacteria. J. Biol. Chem. 245 (1970) 6170-6175. [PMID: 5484472]
Accepted name: heparin-sulfate lyase
Reaction: Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
Other name(s): heparin-sulfate eliminase; heparitin-sulfate lyase; heparitinase I; heparitinase II
Systematic name: heparin-sulfate lyase
Comments: Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-86-1
References:
1. Hovingh, P. and Linker, A. The enzymatic degradation of heparin and heparitin sulfate. 3. Purification of a heparitinase and a heparinase from flavobacteria. J. Biol. Chem. 245 (1970) 6170-6175. [PMID: 5484472]
Accepted name: pectate disaccharide-lyase
Reaction: (1,4-α-D-galacturonosyl)n = (1,4-α-D-galacturonosyl)n-2 + 4-(4-deoxy-α-D-galact-4-enuronosyl)-D-galacturonate
For diagram click here.
Other name(s): pectate exo-lyase; exopectic acid transeliminase; exopectate lyase; exopolygalacturonic acid-trans-eliminase; PATE; exo-PATE; exo-PGL; exopolygalacturonate lyase (ambiguous); pelW (gene name); pelX (gene name)
Systematic name: (1→4)-α-D-galacturonan reducing-end-disaccharide-lyase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-87-2
References:
1. Macmillan, J.D. and Vaughn, R.H. Purification and properties of a polygalacturonic acid-trans-eliminase produced by Clostridium multifermentans. Biochemistry 3 (1964) 564-572. [PMID: 14188174]
2. Shevchik, V.E., Kester, H.C., Benen, J.A., Visser, J., Robert-Baudouy, J. and Hugouvieux-Cotte-Pattat, N. Characterization of the exopolygalacturonate lyase PelX of Erwinia chrysanthemi 3937. J. Bacteriol. 181 (1999) 1652Ð1663. [PMID: 10049400]
3. Shevchik, V.E., Condemine, G., Robert-Baudouy, J. and Hugouvieux-Cotte-Pattat, N. The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J. Bacteriol. 181 (1999) 3912Ð3919. [PMID: 10383957]
Accepted name: pectin lyase
Reaction: Eliminative cleavage of (1→4)-α-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-α-D-galact-4-enuronosyl groups at their non-reducing ends
For diagram click here.
Other name(s): pectin trans-eliminase; endo-pectin lyase; polymethylgalacturonic transeliminase; pectin methyltranseliminase; pectolyase; PL; PNL; PMGL
Systematic name: (1→4)-6-O-methyl-α-D-galacturonan lyase
Comments: Favours pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2, pectate lyase). Demethylation progressively slows its action; it can nevertheless cleave on either side of a demethylated residue if the residue at the other end of the scissile bond is methylated.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-35-6
References:
1. Albersheim, P., Neukom, H. and Deuel, H. Über die Bildung von ungesättigten Abbauprodukten durch ein pekinabbauendes Enzym. Helv. Chim. Acta 43 (1960) 1422-1426.
2. Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J.æ Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5 (1997) 677-689. [PMID: 9195887]
3. Kester, H.C.M and Visser, J. Purification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger. FEMS Microbiol. Lett. 120 (1994) 63-68.
4. Mutenda, K.E., Körner, R., Christensen, T.M.I.E., Mikkelsen, J. and Roepstorff, P. Application of mass spectrometry to determine the activity and specificity of pectin lyase A. Carbohydr.Res. 337 (2002) 1213-1223. [PMID: 12110197]
Accepted name: guluronate-specific alginate lyase
Reaction: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and α-L-guluronate at their reducing end.
Other name(s): alginase II; guluronate lyase; L-guluronan lyase; L-guluronate lyase; poly-α-L-guluronate lyase; polyguluronate-specific alginate lyase; poly(α-L-1,4-guluronide) exo-lyase; poly(α-L-guluronate) lyase; poly[(1→4)-α-L-guluronide] exo-lyase
Systematic name: alginate α-L-guluronate—uronate lyase
Comments: The enzyme catalyses the degradation of alginate by a β-elimination reaction. It cleaves the (1→4) bond between α-L-guluronate and either α-L-guluronate or β-D-mannuronate, generating oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and α-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64177-88-4
References:
1. Boyd, J. and Turvey, J.R. Isolation of poly-α-L-guluronate lyase from Klebsiella aerogenes. Carbohydr. Res. 57 (1977) 163-171. [PMID: 332364]
2. Davidson, I.W., Sutherland, I.W. and Lawson, C.J. Purification and properties of an alginate lyase from a marine bacterium. Biochem. J. 159 (1976) 707-713. [PMID: 1008828]
Accepted name: xanthan lyase
Reaction: Eliminative cleavage of the terminal β-D-mannosyl-(1→4)-β-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-α-L-threo-hex-4-enuronosyl group at the terminus of the side-chain
Systematic name: xanthan lyase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113573-69-6
References:
1. Sutherland, I.W. Xanthan lyases-novel enzymes found in various bacterial species. J. Gen. Microbiol. 133 (1987) 3129-3134. [PMID: 3446747]
Accepted name: exo-(1→4)-α-D-glucan lyase
Reaction: linear α-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
For diagram of reaction click here.
Other name(s): α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase; α-1,4-glucan exo-lyase; α-1,4-glucan lyase; GLase
Systematic name: (1→4)-α-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
Comments: The enzyme catalyses the sequential degradation of (1→4)-α-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an α-glucan containing n (1→4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1→6)-α-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 148710-18-3
References:
1. Yu, S., Kenne, L., Pedersén, M. α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds. Biochim. Biophys. Acta 1156 (1993) 313-320. [PMID: 8461323]
2. Yu, S., Pedersén, M. α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. II. Subcellular localization and partial amino-acid sequence. Planta 191 (1993) 137-142.
3. Yu, S., Ahmad, T., Kenne, L. and Pedersén, M. α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism. Biochim. Biophys. Acta 1244 (1995) 1-9. [PMID: 7766642]
4. Yu, S., Christensen, T.M., Kragh, K.M., Bojsen, K. and Marcussen, J. Efficient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi. Biochim. Biophys. Acta 1339 (1997) 311-320. [PMID: 9187252]
5. Yu, S., Bojsen, K., Svensson, B. and Marcussen, J. α-1,4-glucan lyases producing 1,5-anhydro-D-fructose from starch and glycogen have sequence similarity to α-glucosidases. Biochim. Biophys. Acta 1433 (1999) 1-15. [PMID: 10446355]
6. Lee, S.S., Yu, S. and Withers, S.G. α-1,4-Glucan lyase performs a trans-elimination via a nucleophilic displacement followed by a syn-elimination. J. Am. Chem. Soc. 124 (2002) 4948-4949. [PMID: 11982345]
7. Lee, S.S., Yu, S. and Withers, S.G. Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase. Biochemistry 42 (2003) 13081-13090. [PMID: 14596624]
Accepted name: glucuronan lyase
Reaction: Eliminative cleavage of (1→4)-β-D-glucuronans to give oligosaccharides with 4-deoxy-β-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
For diagram click here.
Other name(s): (1,4)-β-D-glucuronan lyase
Systematic name: (1→4)-β-D-glucuronan lyase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 193766-71-1
References:
1. Michaud, P., Pheulpin, P., Petit, E., Seguin, J.P., Barbotin, J.N., Heyraud, A., Courtois, B. and Courtois, J. Identification of glucuronan lyase from a mutant strain of Rhizobium meliloti. Int. J. Biol. Macromol. 21 (1997) 3-9. [PMID: 9283009]
Accepted name: anhydrosialidase
Reaction: Elimination of α-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-α-N-acetylneuraminate
For diagram click here.
Other name(s): anhydroneuraminidase; sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing); sialidase L
Systematic name: glycoconjugate sialyl-lyase (2,7-cyclizing)
Comments: Also acts on N-glycolylneuraminate glycosides. cf. EC 3.2.1.18 (exo-α-sialidase) and EC 3.2.1.129 (endo-α-sialidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 157857-11-9
References:
1. Li, Y.-T., Nakagawa, H., Ross, S.A., Hansson, G.C. and Li, S.C. A novel sialidase which releases 2,7-anhydro-α-N-acetylneuraminic acid from sialoglycoconjugates. J. Biol. Chem. 265 (1990) 21629-21633. [PMID: 91072361]
Accepted name: levan fructotransferase (DFA-IV-forming)
Reaction: Produces di-β-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2→6)-β-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide
For diagram click here.
Other name(s): 2,6-β-D-fructan D-fructosyl-D-fructosyltransferase (forming di-β-D-fructofuranose 2,6′:2′,6-dianhydride); levan fructotransferase; 2,6-β-D-fructan lyase (di-β-D-fructofuranose-2,6′:2′,6-dianhydride-forming)
Systematic name: (2→6)-β-D-fructan lyase (di-β-D-fructofuranose-2,6′:2′,6-dianhydride-forming)
Comments: This enzyme, like EC 4.2.2.17 [inulin fructotransferase (DFA-I-forming)] and EC 4.2.2.18 [inulin fructotransferase (DFA-III-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 88593-15-1
References:
1. Song, K.B., Bae, K.S., Lee, Y.B., Lee, K.Y. and Rhee, S.K. Characteristics of levan fructotransferase from Arthrobacter ureafaciens K2032 and difructose anhydride IV formation from levan. Enzyme Microb. Technol. 27 (2000) 212-218.
2. Jang, K.H., Ryu, E.J., Park, B.S., Song, K.B., Kang, S.A., Kim, C.H., Uhm, T.B., Park, Y.I. and Rhee, S.K. Levan fructotransferase from Arthrobacter oxydans, J17-21 catalyzes the formation of the di-D-fructose dianhydride IV from levan. J. Agric. Food Chem. 51 (2003) 2632-2636. [PMID: 12696949]
3. Saito, K. and Tomita, F. Difructose anhydrides: Their mass-production and physiological functions. Biosci. Biotechnol. Biochem. 64 (2000) 1321-1327. [PMID: 10945246]
Accepted name: inulin fructotransferase (DFA-I-forming)
Reaction: Produces α-D-fructofuranose β-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2→1)-β-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
For diagram click here.
Other name(s): inulin fructotransferase (DFA-I-producing); inulin fructotransferase (depolymerizing, difructofuranose-1,2':2',1-dianhydride-forming); inulin D-fructosyl-D-fructosyltransferase (1,2':1',2-dianhydride-forming); inulin D-fructosyl-D-fructosyltransferase (forming α-D-fructofuranose β-D-fructofuranose 1,2':1',2-dianhydride); 2,1-β-D-fructan lyase (α-D-fructofuranose-β-D-fructofuranose-1,2':2,1'-dianhydride-forming)
Systematic name: (2→1)-β-D-fructan lyase (α-D-fructofuranose-β-D-fructofuranose-1,2':2,1'-dianhydride-forming)
Comments: This enzyme, like EC 4.2.2.16 [levan fructotransferase (DFA-IV-forming)] and EC 4.2.2.18 [inulin fructotransferase (DFA-III-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 125008-19-7
References:
1. Seki, K., Haraguchi, K., Kishimoto, M., Kobayashi, S. and Kainuma, K. Purification and properties of a novel inulin fructotransferase (DFA I-producing) from Arthrobacter globiformis S14-3. Agric. Biol. Chem. 53 (1989) 2089-2094.
Accepted name: inulin fructotransferase (DFA-III-forming)
Reaction: Produces α-D-fructofuranose β-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2→1)-β-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
For diagram click here.
Other name(s): inulin fructotransferase (DFA-III-producing); inulin fructotransferase (depolymerizing); inulase II; inulinase II; inulin fructotransferase (depolymerizing, difructofuranose-1,2':2,3'-dianhydride-forming); inulin D-fructosyl-D-fructosyltransferase (1,2':2,3'-dianhydride-forming); inulin D-fructosyl-D-fructosyltransferase (forming α-D-fructofuranose β-D-fructofuranose 1,2':2,3'-dianhydride)
Systematic name: 2,1-β-D-fructan lyase (α-D-fructofuranose-β-D-fructofuranose-1,2':2,3'-dianhydride-forming)
Comments: This enzyme, like EC 4.2.2.16 [levan fructotransferase (DFA-IV-forming)] and EC 4.2.2.17 [inulin fructotransferase (DFA-I-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50936-42-0
References:
1. Uchiyama, T. Action of Arthrobacter ureafaciens inulinase II on several oligofructans and bacterial levans. Biochim. Biophys. Acta 397 (1975) 153-163. [PMID: 1148257]
2. Uchiyama, T., Niwa, S. and Tanaka, K. Purification and properties of Arthrobacter ureafaciens inulase II. Biochim. Biophys. Acta 315 (1973) 412-420.
Accepted name: chondroitin B lyase
Reaction: Eliminative cleavage of dermatan sulfate containing (1→4)-β-D-hexosaminyl and (1→3)-β-D-glucurosonyl or (1→3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (ΔUA-GalNAc-4S).
Glossary: dermatan sulfate = chondroitin sulfate B
For the nomenclature of glycoproteins, glycopeptides and peptidoglycans, click here
Other name(s): chondroitinase B; ChonB; ChnB
Systematic name: chondroitin B lyase
Comments: This is the only lyase that is known to be specific for dermatan sulfate as substrate. The minimum substrate length required for catalysis is a tetrasaccharide [2]. 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].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52227-83-5
References:
1. Gu, K., Linhardt, R.J., Laliberte, M., Gu, K. and Zimmermann, J. Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum. Biochem. J. 312 (1995) 569-577. [PMID: 8526872]
2. Pojasek, K., Raman, R., Kiley, P., Venkataraman, G. and Sasisekharan, R. Biochemical characterization of the chondroitinase B active site. J. Biol. Chem. 277 (2000) 31179-31186. [PMID: 12063249]
3. 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. [PMID: 11500043]
4. Suzuki, K., Terasaki, Y. and Uyeda, M. Inhibition of hyaluronidases and chondroitinases by fatty acids. J. Enzyme Inhib. Med. Chem. 17 (2002) 183-186. [PMID: 12443044]
5. Ototani, N. and Yosizawa, Z. Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4B. Carbohydr. Res. 70 (1979) 295-306. [PMID: 427837]
6. Tkalec, A.L., Fink, D., Blain, F., Zhang-Sun, G., Laliberte, M., Bennett, D.C., Gu, K., Zimmermann, J.J. and Su, H. Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum. Appl. Environ. Microbiol. 66 (2000) 29-35. [PMID: 10618199]
7. Michel, G., Pojasek, K., Li, Y., Sulea, T., Linhardt, R.J., Raman, R., Prabhakar, V., Sasisekharan, R. and Cygler, M. The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery. J. Biol. Chem. 279 (2004) 32882-32896. [PMID: 15155751]
8. Li, Y., Matte, A., Su, H. and Cygler, M. Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1055-1057. [PMID: 10216304]
9. Huang, W., Matte, A., Li, Y., Kim, Y.S., Linhardt, R.J., Su, H. and Cygler, M. Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 Å resolution. J. Mol. Biol. 294 (1999) 1257-1269. [PMID: 10600383]
10. 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. [PMID: 16336265]
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 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. [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. [PMID: 16336265]
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 C4—C5 bond on the hexuronic acid moiety of the products [4,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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. [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. [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. [PMID: 18992215]
Accepted name: pectate trisaccharide-lyase
Reaction: eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
Other name(s): exopectate-lyase; pectate lyase A; PelA
Systematic name: (1→4)-α-D-galacturonan reducing-end-trisaccharide-lyase
Comments: Differs in specificity from EC 4.2.2.9, pectate disaccharide-lyase, as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end. Disaccharides and tetrasaccharides may also be removed [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kluskens, L.D., van Alebeek, G.J., Voragen, A.G., de Vos, W.M. and van der Oost, J. Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima. Biochem. J. 370 (2003) 651-659. [PMID: 12443532]
2. Tamaru, Y. and Doi, R.H. Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome. Proc. Natl. Acad. Sci. USA 98 (2001) 4125-4129. [PMID: 11259664]
3. Berensmeier, S., Singh, S.A., Meens, J. and Buchholz, K. Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase. Appl. Microbiol. Biotechnol. 64 (2004) 560-567. [PMID: 14673544]
Accepted name: rhamnogalacturonan endolyase
Reaction: Endotype eliminative cleavage of L-α-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
For diagram of reaction click here.
Other name(s): rhamnogalacturonase B; α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronide lyase; Rgase B; rhamnogalacturonan α-L-rhamnopyranosyl-(1,4)-α-D-galactopyranosyluronide lyase; RG-lyase; YesW; RGL4; Rgl11A; Rgl11Y; RhiE
Systematic name: α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate endolyase
Comments: The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mutter, M., Colquhoun, I.J., Schols, H.A., Beldman, G. and Voragen, A.G. Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronide lyase. Plant Physiol. 110 (1996) 73-77. [PMID: 8587995]
2. Azadi, P., O'Neill, M.A., Bergmann, C., Darvill, A.G. and Albersheim, P. The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase. Glycobiology 5 (1995) 783-789. [PMID: 8720076]
3. Mutter, M., Colquhoun, I.J., Beldman, G., Schols, H.A., Bakx, E.J. and Voragen, A.G. Characterization of recombinant rhamnogalacturonan α-L-rhamnopyranosyl-(1,4)-α-D-galactopyranosyluronide lyase from Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I regions of pectin. Plant Physiol. 117 (1998) 141-152. [PMID: 9576783]
4. Kadirvelraj, R., Harris, P., Poulsen, J.C., Kauppinen, S. and Larsen, S. A stepwise optimization of crystals of rhamnogalacturonan lyase from Aspergillus aculeatus. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 1346-1349. [PMID: 12136151]
5. Laatu, M. and Condemine, G. Rhamnogalacturonate lyase RhiE is secreted by the out system in Erwinia chrysanthemi. J. Bacteriol. 185 (2003) 1642-1649. [PMID: 12591882]
6. Pages, S., Valette, O., Abdou, L., Belaich, A. and Belaich, J.P. A rhamnogalacturonan lyase in the Clostridium cellulolyticum cellulosome. J. Bacteriol. 185 (2003) 4727-4733. [PMID: 12896991]
7. Ochiai, A., Yamasaki, M., Itoh, T., Mikami, B., Hashimoto, W. and Murata, K. Crystallization and preliminary X-ray analysis of the rhamnogalacturonan lyase YesW from Bacillus subtilis strain 168, a member of polysaccharide lyase family 11. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 438-440. [PMID: 16682770]
8. Jensen, M.H., Otten, H., Christensen, U., Borchert, T.V., Christensen, L.L., Larsen, S. and Leggio, L.L. Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from Aspergillus aculeatus. J. Mol. Biol. 404 (2010) 100-111. [PMID: 20851126]
Accepted name: rhamnogalacturonan exolyase
Reaction: Exotype eliminative cleavage of α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosacharides containing α-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
For diagram of reaction click here.
Glossary: 6-deoxy-2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-mannopyranose =
2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-rhamnopyranose
Other name(s): YesX
Systematic name: α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate exolyase
Comments: The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ochiai, A., Itoh, T., Mikami, B., Hashimoto, W. and Murata, K. Structural determinants responsible for substrate recognition and mode of action in family 11 polysaccharide lyases. J. Biol. Chem. 284 (2009) 10181-10189. [PMID: 19193638]
2. Ochiai, A., Itoh, T., Kawamata, A., Hashimoto, W. and Murata, K. Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization. Appl. Environ. Microbiol. 73 (2007) 3803-3813. [PMID: 17449691]
Accepted name: gellan lyase
Reaction: Eliminative cleavage of β-D-glucopyranosyl-(1→4)-β-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-β-D-Glcp.
Systematic name: gellan β-D-glucopyranosyl-(1→4)-D-glucopyranosyluronate lyase
Comments: The enzyme is highly specific to gellan, especially deacetylated gellan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hashimoto, W., Maesaka, K., Sato, N., Kimura, S., Yamamoto, K., Kumagai, H. and Murata, K. Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1. Arch. Biochem. Biophys. 339 (1997) 17-23. [PMID: 9056228]
2. Hashimoto, W., Sato, N., Kimura, S. and Murata, K. Polysaccharide lyase: molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1. Arch. Biochem. Biophys. 354 (1998) 31-39. [PMID: 9633595]
3. Miyake, O., Kobayashi, E., Nankai, H., Hashimoto, W., Mikami, B. and Murata, K. Posttranslational processing of polysaccharide lyase: maturation route for gellan lyase in Bacillus sp. GL1. Arch. Biochem. Biophys. 422 (2004) 211-220. [PMID: 14759609]
Accepted name: oligo-alginate lyase
Reaction: Cleavage of 4-deoxy-α-L-erythro-hex-4-enopyranuronoside oligosaccharides into 4-deoxy-α-L-erythro-hex-4-enopyranuronate monosaccharides.
Other name(s): aly (gene name) (ambiguous); oalS17 (gene name); oligoalginate lyase; exo-oligoalginate lyase
Systematic name: alginate oligosaccharide 4-deoxy-α-L-erythro-hex-4-enopyranuronate-(1→4)-hexananopyranuronate lyase
Comments: The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left.The enzyme catalyses a β-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hashimoto, W., Miyake, O., Momma, K., Kawai, S. and Murata, K. Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J. Bacteriol. 182 (2000) 4572-4577. [PMID: 10913091]
2. Kim, H.T., Chung, J.H., Wang, D., Lee, J., Woo, H.C., Choi, I.G. and Kim, K.H. Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40. Appl. Microbiol. Biotechnol. 93 (2012) 2233-2239. [PMID: 22281843]
3. Jagtap, S.S., Hehemann, J.H., Polz, M.F., Lee, J.K. and Zhao, H. Comparative biochemical characterization of three exolytic oligoalginate lyases from Vibrio splendidus reveals complementary substrate scope, temperature, and pH adaptations. Appl. Environ. Microbiol. 80 (2014) 4207-4214. [PMID: 24795372]
4. Wang, L., Li, S., Yu, W. and Gong, Q. Cloning, overexpression and characterization of a new oligoalginate lyase from a marine bacterium, Shewanella sp. Biotechnol. Lett. 37 (2015) 665-671. [PMID: 25335746]
Accepted name: pectin monosaccharide-lyase
Reaction: (1,4-α-D-galacturonosyl methyl ester)n = (1,4-α-D-galacturonosyl methyl ester)n-1 + 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate
Other name(s): exo-pectin lyase; PLIII
Systematic name: poly(1,4-α-D-galacturonosyl methyl ester) non-reducing-end-monosaccharide-lyase
Comments: The enzyme, isolated from the fungus Aspergillus giganteus, acts on the non-reducing end of methyl-esterified polygalacturonan, releasing either 4-deoxy--L-threo-hex-4-enopyranuronate or 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate. The enzyme is stimulated by divalent cations, with Co2+ having the strongest effect. It is able to act on substrates as short as a disaccharide, and was active on substrates with degrees of methyl esterification ranging between 34% and 90%.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Pedrolli, D.B. and Carmona, E.C. Purification and characterization of a unique pectin lyase from Aspergillus giganteus able to release unsaturated monogalacturonate during pectin degradation. Enzyme Res. 2014 (2014) 353915. [PMID: 25610636]
Accepted name: α-L-rhamnosyl-(1→4)-D-glucuronate lyase
Reaction: α-L-rhamnosyl-(1→4)-D-glucuronate = L-rhamnopyranose + 4-deoxy-L-threo-hex-4-enopyranuronate
Other name(s): L-rhamnose-α-1,4-D-glucuronate lyase; FoRham (gene name)
Systematic name: α-L-rhamnosyl-(1→4)-D-glucuronate lyase
Comments: The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from α-L-rhamnosyl-(1→4)-D-glucuronate or (with lower activity) from oligosaccharides that contain this motif at the non-reducing end, leaving an unsaturated glucuronate residue. Among its natural substrates is the type II arabinogalactan component of gum arabic.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Kondo, T., Kichijo, M., Maruta, A., Nakaya, M., Takenaka, S., Arakawa, T., Fushinobu, S. and Sakamoto, T. Structural and functional analysis of gum arabic L-rhamnose-α-1,4-D-glucuronate lyase establishes a novel polysaccharide lyase family. J. Biol. Chem. 297 (2021) 101001. [PMID: 34303708]
Accepted name: peptidoglycan lytic transglycosylase
Reaction: a peptidoglycan chain = a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-(peptide) at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end
Other name(s): lytic murein transglycosylase; endolytic murein transglycosylase; lytic transglycosylase; endolytic transglycosylase; MtlA; MltB; MltC; MltD; MltE; MltF; MltG; Slt; RlpA; SleB; SpoIID
Systematic name: peptidoglycan N-acetylmuramate—N-acetyl-β-D-glucosamine lyase
Comments: A group of bacterial enzymes that catalyse the non-hydrolytic cleavage of peptidoglycan (PG). The enzymes fragment the polysaccharide chain at the β-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues by an intramolecular cyclization of the N-acetylmuramyl moiety to yield a 1,6-anhydro-N-acetyl-β-D-muramyl product. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand. The MtlG enzyme of Gram-negative bacteria may function to regulate glycan strand length within the PG polymer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Holtje, J.V., Mirelman, D., Sharon, N. and Schwarz, U. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124 (1975) 1067-1076. [PMID: 357]
2. Yunck, R., Cho, H. and Bernhardt, T.G. Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria. Mol. Microbiol. 99 (2016) 700-718. [PMID: 26507882]
3. Dik, D.A., Marous, D.R., Fisher, J.F. and Mobashery, S. Lytic transglycosylases: concinnity in concision of the bacterial cell wall. Crit. Rev. Biochem. Mol. Biol. 52 (2017) 503-542. [PMID: 28644060]