Vitamin K-dependent carboxylation. Mechanistic studies with 3-fluoroglutamate-containing substrates.
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.
Vidal-Cros
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Laboratoire de Chimie Organique Biologique, C.N.R.S. U.A. 493, Université Paris, France.
Gaudry
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Marquet
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D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D005971:Glutamates; D007536:Isomerism; D008862:Microsomes, Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides; D051381:Rats; D014812:Vitamin K
D005971:Glutamates; D009842:Oligopeptides; D014812:Vitamin K; C063592:t-butyloxycarbonyl-3-fluoroglutamyl-glutamyl-valine; C046739:3-fluoroglutamate