Stereochemical studies on a plasmid-coded fluoroacetate halidohydrolase
1984; Elsevier BV; Volume: 12; Issue: 3 Linguagem: Inglês
10.1016/0045-2068(84)90003-8
ISSN1090-2120
AutoresKarin G. Au, Christopher T. Walsh,
Tópico(s)Amino Acid Enzymes and Metabolism
ResumoThe stereochemical course of action of haloacetate halidohydrolase H-1 from Pseudomonas sp., strain A, which catalyzes the dehalogenation of fluoroacetate to glycolate, has been determined by enzymatic analysis of products from incubations with both enantiomers of 20-fluoropropionate, and by 1H NMR analysis of the ester of (−)-α-methoxy-α-(trifluoromethyl)phenylacetic acid with phenacyl [2-2H1]glycolate derived from the product of incubation with the (S)-monodeuterofluoroacetate. The results support a direct displacement mechanism for this enzyme, since they indicate that the reaction is catalyzed with inversion of configuration.
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