An Epoxide Intermediate in Glycosidase Catalysis
نویسندگان
چکیده
منابع مشابه
Catalysis of potato epoxide hydrolase, StEH1.
The kinetic mechanism of epoxide hydrolase (EC 3.3.2.3) from potato, StEH1 (Solanum tuberosum epoxide hydrolase 1), was studied by presteady-state and steady-state kinetics as well as by pH dependence of activity. The specific activities towards the different enantiomers of TSO (trans-stilbene oxide) as substrate were 43 and 3 micromol x min(-1) x mg(-1) with the R,R- or S,S-isomers respectivel...
متن کاملDirect observation of an enamine intermediate in amine catalysis.
An enamine intermediate is believed to be the central feature of biological catalysts, such as aldolases and small molecule amine organocatalysts. Despite decades of investigation of naturally occurring aldolase enzymes and recent studies on designed aldolase antibodies and organocatalysts, direct structural observation of an enamine intermediate has proven to be rare. Herein, we report the obs...
متن کاملEnantioselective linchpin catalysis by SOMO catalysis: an approach to the asymmetric alpha-chlorination of aldehydes and terminal epoxide formation.
Time for SOme MOre: For the first time SOMO (singly occupied molecular orbital) activation has been exploited to allow a new approach to the alpha-chlorination of aldehydes. This transformation can be readily implemented as part of a linchpin catalysis approach to the enantioselective production of terminal epoxides.
متن کاملInactivation of epoxide hydrolase by catalysis-induced formation of isoaspartate.
Epoxide hydrolases catalyze hydrolytic epoxide ring-opening, most often via formation of a covalent hydroxyalkyl-enzyme intermediate. A mutant of Agrobacterium radiobacter epoxide hydrolase, in which the phenylalanine residue that flanks the invariant catalytic aspartate nucleophile is replaced by a threonine, exhibited inactivation during conversion when the (R)-enantiomer of para-nitrostyrene...
متن کاملStructure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis.
The X-ray crystal structure of human soluble epoxide hydrolase (sEH) has been determined at 2.6 A resolution, revealing a domain-swapped quaternary structure identical to that observed for the murine enzyme [Argiriadi, M. A., Morisseau, C., Hammock, B. D., and Christianson, D. W. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 10637-10642]. As with the murine enzyme, the epoxide hydrolytic mechanism o...
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ژورنال
عنوان ژورنال: ACS Central Science
سال: 2020
ISSN: 2374-7943,2374-7951
DOI: 10.1021/acscentsci.0c00111