Mannosidases

Far less well understood is the observation that many bacterial species, predominantly but not exclusively pathogens and symbionts, also possess putative GH38 α − mannosidases whose activity and specificity is unknown. ❋ Michael D. L. Suits Et Al. (2010)

Figure 3a, typical for many α − mannosidases whose lack of α − 1,2 mannosidase activity prevents access to these masked substrates. ❋ Michael D. L. Suits Et Al. (2010)

Catalysis around this area of the conformational sphere has also been proposed, recently, for inverting GH92 α − mannosidases ❋ Michael D. L. Suits Et Al. (2010)

Of particular relevance to the study described here, are the GH38 α − mannosidases. ❋ Michael D. L. Suits Et Al. (2010)

The paucity of information on the α − mannosidases from these pathogenic bacteria, led us to study the ❋ Michael D. L. Suits Et Al. (2010)

Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, et al. (2005) Mechanism of class 1 (Glycosylhydrolase family 47) alpha-mannosidases involved in ❋ Michael D. L. Suits Et Al. (2010)

Kuntz DA, Hoffman D, Janzer RC, Gerber-Lemaire S, et al. (2008) Functionalized pyrrolidine inhibitors of human type II alpha-mannosidases as anti-cancer agents: Optimizing the fit to the active site. ❋ Michael D. L. Suits Et Al. (2010)

GH38 α − mannosidases are known to act with net retention of anomeric configuration; a mechanism in which a glycosyl-enzyme intermediate is flanked by oxocarbenium-ion like transition-states. ❋ Michael D. L. Suits Et Al. (2010)

Thompson AJ, Chavan S, Dinev Z, et al. (2009) Mechanistic insights into a calcium-dependent family of mannosidases in a human gut symbiont. ❋ Michael D. L. Suits Et Al. (2010)

The three-dimensional structure of two GH92 mannosidases defines a family of two-domain proteins in which the catalytic center is located at the domain interface, providing acid (glutamate) and base (aspartate) assistance to hydrolysis in a Ca ❋ Yanping Zhu (2010)

[37] and a GH1 "putative β − glucosidase" (a family that includes varied β − D glycoside hydrolases including glucosidases, mannosidases, galactosidases and glucuronidases). ❋ Michael D. L. Suits Et Al. (2010)

β − mannosidases in which β-linked substrate complexes have been observed in the ❋ Michael D. L. Suits Et Al. (2010)