Structural highlights
Function
EBDG_AMYOR Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The synthesis of amino-derivatives of castanospermine and australine and their characterisation as inhibitors of the exo-beta-D-glucosaminidase CsxA through enzyme kinetics and X-ray structural analysis is described.
Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue.,Pluvinage B, Ghinet MG, Brzezinski R, Boraston AB, Stubbs KA Org Biomol Chem. 2009 Oct 21;7(20):4169-72. Epub 2009 Aug 14. PMID:19795054[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cote N, Fleury A, Dumont-Blanchette E, Fukamizo T, Mitsutomi M, Brzezinski R. Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem J. 2006 Mar 15;394(Pt 3):675-86. PMID:16316314 doi:http://dx.doi.org/10.1042/BJ20051436
- ↑ Nanjo F, Katsumi R, Sakai K. Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J Biol Chem. 1990 Jun 15;265(17):10088-94. PMID:2351651
- ↑ Pluvinage B, Ghinet MG, Brzezinski R, Boraston AB, Stubbs KA. Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue. Org Biomol Chem. 2009 Oct 21;7(20):4169-72. Epub 2009 Aug 14. PMID:19795054 doi:10.1039/b913235j
