6b9o
Structure of GH 38 Jack Bean alpha-mannosidase
Structural highlights
FunctionMANA_CANEN Liberates mannose from p-nitrophenyl-alpha-D-mannoside (PubMed:1156387, PubMed:12325362, PubMed:4973951). Liberates mannose from further alpha-D-mannosides including methyl-, benzyl-alpha-D-mannoside, 1-6-linked di-, tri- and tetrasaccharides of alpha-D-mannose and mannosyl-rhamnose (PubMed:12325362). Liberates mannose from various glycoproteins like ovalbumin and ovomucoid (PubMed:12325362, PubMed:5145). Does not hydrolyze beta-D-mannosides (PubMed:12325362). Has glycosyltransferase activity, forming disaccharides from mannose and lyxose but not from glucose, galactose, ribose, xylose or arabinose (PubMed:12325362).[1] [2] [3] [4] Publication Abstract from PubMedMultivalent design of glycosidase inhibitors is a promising strategy for the treatment of diseases involving enzymatic hydrolysis of glycosidic bonds in carbohydrates. An essential prerequisite for successful applications is the atomic-level understanding of how outstanding binding enhancement occurs with multivalent inhibitors. Herein we report the first high-resolution crystal structures of the Jack bean alpha-mannosidase (JBalpha-man) in apo and inhibited states. The three-dimensional structure of JBalpha-man in complex with the multimeric cyclopeptoid-based inhibitor displaying the largest binding enhancements reported so far provides decisive insight into the molecular mechanisms underlying multivalent effects in glycosidase inhibition. Structural Basis of Outstanding Multivalent Effects in Jack Bean alpha-Mannosidase Inhibition.,Howard E, Cousido-Siah A, Lepage ML, Schneider JP, Bodlenner A, Mitschler A, Meli A, Izzo I, Alvarez HA, Podjarny A, Compain P Angew Chem Int Ed Engl. 2018 Jul 2;57(27):8002-8006. doi: 10.1002/anie.201801202., Epub 2018 Jun 6. PMID:29722924[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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