Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.
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.
Offen
Wendy A
WA
Department of Chemistry, The University of York, Heslington, UK.
Zechel
David L
DL
Withers
Stephen G
SG
Gilbert
Harry J
HJ
Davies
Gideon J
GJ
D001439:Bacteroides / Q000201:enzymology; D006868:Hydrolysis; D008362:Mannosides / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D013816:Thermodynamics; D044902:beta-Mannosidase / Q000737:chemistry* / Q000378:metabolism
D008362:Mannosides; D044902:beta-Mannosidase