Affiliation:
1. Laboratoire de Chimie Organique Biologique, C.N.R.S. U.A. 493, Université Paris 6, Tour 44/45 (3éme Étage), 4 Place Jussieu, 75252 Paris CEDEX 05, France
Abstract
The tripeptides t-butyloxycarbonyl-Xaa-Glu-[3H]Val, where Xaa is either (2R,3S)- or (2R,3R)-3-fluoroglutamate (respectively the erythro and the threo isomer), were synthesized and their behaviour during vitamin K-dependent carboxylation was studied. Neither peptide was carboxylated. The erythro compound gave rise to an HF-elimination product representing 1% of the starting material. This HF elimination did not occur during incubation of the threo compound. The formation of the dehydropeptide, probably by elimination of an F- anion from an intermediate carbanion, favours the ionic pathway for vitamin K-dependent carboxylation.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
12 articles.
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