Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.

Article Details

Citation

Offen WA, Zechel DL, Withers SG, Gilbert HJ, Davies GJ

Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.

Chem Commun (Camb). 2009 May 14;(18):2484-6. doi: 10.1039/b902240f. Epub 2009 Apr 6.

PubMed ID
19532864 [ View in PubMed
]
Abstract

The 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Beta-mannosidaseQ8AAK6Details