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 126.96.36.199 and EC 188.8.131.52) 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, CAS registry number:
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]