Catalysis of potato epoxide hydrolase, StEH1
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 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 کاملConformational diversity and enantioconvergence in potato epoxide hydrolase 1
a Potato epoxide hydrolase 1 (StEH1) is a biocatalytically important enzyme that exhibits rich enantio-and regioselectivity in the hydrolysis of chiral epoxide substrates. In particular, StEH1 has been demonstrated to enantioconvergently hydrolyze racemic mixes of styrene oxide (SO) to yield (R)-1-phenylethanediol. This work combines computational, crystallographic and biochemical analyses to u...
متن کاملHysteretic Behavior, Regioselectivity and Role of Salt Bridging Residues at the Domain Interface of Potato Epoxide Hydrolase StEH1, Site-Directed Mutagenesis and Kinetic Study
According to an earlier study, StEH1 exhibits slow transitions between different conformational states implying hysteresis. Since, ionic interactions play a great role in protein stability, they are also expected to have significant effects on the structure dynamics of protein. The aim of this work is to remove some ionic interactions from the domain interface of StEH1 and investigate its effec...
متن کاملMicrosomal epoxide hydrolase polymorphisms.
Microsomal epoxide hydrolase plays a dual role in the activation and detoxification of carcinogenic compounds. Two polymorphic sites have been described in exons 3 and 4 of the microsomal epoxide hydrolase gene that change tyrosine residue 113 to histidine (Tyr113His) and histidine 139 to arginine (His139Arg), respectively. The exon 3 polymorphism reduces enzyme activity by approximately 50%, w...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2005
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20050526