ExplorEnz: EC 4.2.2.*

Your query returned 28 entries. Printable version

4.2.2.1

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 (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous)

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. [PMID: 13762462]
2.	Meyer, K. and Rapport, M.M. Hyaluronidases. Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199–236. [PMID: 14943668]
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. [DOI] [PMID: 5642600]

[EC 4.2.2.1 created 1961 as EC 4.2.99.1, transferred 1972 to EC 4.2.2.1, modified 2001]

4.2.2.2

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 of reaction, 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. [DOI] [PMID: 13860094]
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. [PMID: 14235514]
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. [PMID: 14235515]
4.	Nagel, C.W. and Vaughn, R.H. The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa. Arch. Biochem. Biophys. 94 (1961) 328. [DOI] [PMID: 13727438]
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. [DOI] [PMID: 9195887]

[EC 4.2.2.2 created 1965 as EC 4.2.99.3, transferred 1972 to EC 4.2.2.2, modified 2002]

4.2.2.3

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. [DOI] [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 4.2.2.3 created 1965 as EC 4.2.99.4, transferred 1972 to EC 4.2.2.3, modified 1990, modified 2015]

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]

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)]

4.2.2.6

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. [DOI] [PMID: 5671040]

[EC 4.2.2.6 created 1972, modified 2010]

4.2.2.7

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]

[EC 4.2.2.7 created 1972]

4.2.2.8

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]

[EC 4.2.2.8 created 1972]

4.2.2.9

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 of reaction, 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

Comments:

The enzyme catalyses the eliminative cleavage of an unsaturated disaccharide from the reducing end of homogalacturonan (the backbone of smooth regions of pectate, also known as de-esterified pectin).

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) 1652–1663. [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) 3912–3919. [PMID: 10383957]

[EC 4.2.2.9 created 1972, modified 2002]

4.2.2.10

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 of reaction, 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. 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. [DOI] [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. [DOI] [PMID: 12110197]

[EC 4.2.2.10 created 1972, modified 2002]

4.2.2.11

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]

[EC 4.2.2.11 created 1990, modified 2015]

4.2.2.12

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. [DOI] [PMID: 3446747]

[EC 4.2.2.12 created 1990]

4.2.2.13

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 the anhydrofructose pathway, 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. Other enzymes involved in the anhydrofructose 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. [DOI] [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. [PMID: 7763826]
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14596624]

[EC 4.2.2.13 created 1999]

4.2.2.14

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 of reaction, 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. [DOI] [PMID: 9283009]

[EC 4.2.2.14 created 2000]

4.2.2.15

Accepted name:

anhydrosialidase

Reaction:

Elimination of α-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-α-N-acetylneuraminate

For diagram of reaction, 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: 2254319]

[EC 4.2.2.15 created 1992 as EC 3.2.1.138, transferred 2003 to EC 4.2.2.15]

4.2.2.16

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 of reaction, 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. [DOI] [PMID: 10899545]
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, J 17-21 catalyzes the formation of the di-D-fructose dianhydride IV from levan. J. Agric. Food Chem. 51 (2003) 2632–2636. [DOI] [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]

[EC 4.2.2.16 created 2004]

4.2.2.17

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 of reaction, 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.

[EC 4.2.2.17 created 1992 as EC 2.4.1.200, transferred 2004 to EC 4.2.2.17]

4.2.2.18

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 of reaction, 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); 2,1-β-D-fructan lyase (α-D-fructofuranose-β-D-fructofuranose-1,2′:2,3′-dianhydride-forming)

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, PDB, 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. [DOI] [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.

[EC 4.2.2.18 created 1976 as EC 2.4.1.93, transferred 2004 to EC 4.2.2.18]

4.2.2.19

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:

chondroitin sulfate B = dermatan sulfate
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. [DOI] [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. [DOI] [PMID: 11500043]
4.	Suzuki, K., Terasaki, Y. and Uyeda, M. Inhibition of hyaluronidases and chondroitinases by fatty acids. J. Enzyme 17 (2002) 183–186. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 16336265]

[EC 4.2.2.19 created 2005]

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))]

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:

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:

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. [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]

4.2.2.22

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

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14673544]

[EC 4.2.2.22 created 2007]

4.2.2.23

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.

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

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 20851126]

[EC 4.2.2.23 created 2011]

4.2.2.24

Accepted name:

rhamnogalacturonan exolyase

Reaction:

Exotype eliminative cleavage of α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosaccharides 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 ramnosylgalacturan degradation, 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

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. [DOI] [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. [DOI] [PMID: 17449691]

[EC 4.2.2.24 created 2011]

4.2.2.25

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

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14759609]

[EC 4.2.2.25 created 2011]

4.2.2.26

Accepted name:

oligo-alginate lyase

Reaction:

Cleavage of poly(4-deoxy-α-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends 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

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 25335746]

[EC 4.2.2.26 created 2015]

4.2.2.27

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

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. 2014:353915 (2014). [PMID: 25610636]

[EC 4.2.2.27 created 2020]

4.2.2.28

Accepted name:

α-L-rhamnosyl-(1→4)-β-D-glucuronate lyase

Reaction:

an α-L-rhamnose-(1→4)-β-D-glucuronide = α-L-rhamnopyranose + a 4-deoxy-α-L-threo-hex-4-enopyranuronoside

Other name(s):

L-rhamnose-α-1,4-D-glucuronate lyase; FoRham (gene name)

Systematic name:

α-L-rhamnosyl-(1→4)-β-D-glucuronate lyase

Comments:

The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from α-L-rhamnosyl-(1→4)-β-D-glucuronate or 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

References:

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. 297:101001 (2021). [DOI] [PMID: 34303708]

[EC 4.2.2.28 created 2022]