2wbk
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Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Michaelis complex of the beta-mannosidase Man2A shows distortion to a (1)S(5) conformation adding to the growing body of evidence supporting catalysis through a boat conformation. Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.,Offen WA, Zechel DL, Withers SG, Gilbert HJ, Davies GJ Chem Commun (Camb). 2009 May 14;(18):2484-6. Epub 2009 Apr 6. PMID:19532864[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 15:50, 13 December 2023.