Structural highlights
Function
GLMA_THEKO Exo-type enzyme that specifically cleaves the non-reducing terminal glycosidic bond of chitooligosaccharides (PubMed:12923090, PubMed:15136574, PubMed:28130448). Catalyzes the hydrolysis of GlcN-GlcNAc to glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) (PubMed:15136574, PubMed:28130448). Involved in chitin degradation (PubMed:12923090, PubMed:15136574). Can also hydrolyze reduced chitobiose (GlcN2OH) and chitooligosaccharides of various chain lengths (PubMed:12923090).[1] [2] [3]
References
- ↑ Tanaka T, Fukui T, Atomi H, Imanaka T. Characterization of an exo-beta-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Bacteriol. 2003 Sep;185(17):5175-81. PMID:12923090 doi:10.1128/JB.185.17.5175-5181.2003
- ↑ Tanaka T, Fukui T, Fujiwara S, Atomi H, Imanaka T. Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem. 2004 Jul 16;279(29):30021-7. PMID:15136574 doi:10.1074/jbc.M314187200
- ↑ Mine S, Watanabe M, Kamachi S, Abe Y, Ueda T. The Structure of an Archaeal β-Glucosaminidase Provides Insight into Glycoside Hydrolase Evolution. J Biol Chem. 2017 Mar 24;292(12):4996-5006. PMID:28130448 doi:10.1074/jbc.M116.766535