Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.

@article{Zhu2010MechanisticII,
  title={Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.},
  author={Yanping Zhu and Michael D Suits and Andrew J. Thompson and Sambhaji P. Chavan and Zoran Dinev and Claire Dumon and Nicola L. Smith and Kelley W. Moremen and Yong Xiang and Aloysius H Siriwardena and Spencer J Williams and Harry J. Gilbert and Gideon J. Davies},
  journal={Nature chemical biology},
  year={2010},
  volume={6 2},
  pages={
          125-32
        }
}
Colonic bacteria, exemplified by Bacteroides thetaiotaomicron, play a key role in maintaining human health by harnessing large families of glycoside hydrolases (GHs) to exploit dietary polysaccharides and host glycans as nutrients. Such GH family expansion is exemplified by the 23 family GH92 glycosidases encoded by the B. thetaiotaomicron genome. Here we show that these are alpha-mannosidases that act via a single displacement mechanism to utilize host N-glycans. The three-dimensional… Expand
Analysis of a New Family of Widely Distributed Metal-independent α-Mannosidases Provides Unique Insight into the Processing of N-Linked Glycans*
TLDR
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Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164
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TLDR
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TLDR
Evidence that nature has evolved a small set of common mechanisms that unite almost all of these mannosidase families is discussed, including β-1,2-mannosyltransferases/phosphorylases that perform mannosyl transfer through a boat conformation as well as some mannosideases that are metalloenzymes and require divalent cations for catalysis. Expand
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