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Synthesis of peptide analogues of prothrombin precursor sequence 5-9. Substrate specificity of vitamin K dependent carboxylase.

Abstract：

:Thirty-five analogues of Phe-Leu-Glu-Glu-Leu, the pentapeptide sequence 5-9 of bovine prothrombin precursor, were synthesized and assayed as potential substrates or inhibitors of rat liver vitamin K dependent carboxylase. Carboxylation of substrate was determined by measuring the incorporation of carbon-24 labeled bicarbonate into product. Changes in substrate carboxylation produced by changing peptide chain length, amino acid chirality, or the distance separating the peptide chain backbone from the carboxyl group were measured. The data suggest that the carboxylase carboxylates L-glutamic acid residues and does not carboxylate L-aspartic acid, L-homoglutamic acid, glutamine, or D-glutamic acid residues; tri-through pentapeptides are better substrates than mono- or bis(amino acid) derivatives, and hydrophobic groups added to the N-terminus can produce better substrates for the enzyme. None of the synthetic substrates is carboxylated as effectively as the endogenous protein substrates for the enzyme. The effect of structure on additional parameters affecting carboxylation is discussed.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Rich DH,Lehrman SR,Kawai M,Goodman HL,Suttie JW

doi

10.1021/jm00138a013

subject

Has Abstract

pub_date

1981-06-01 00:00:00

pages

706-11

issue

6

eissn

0022-2623

issn

1520-4804

journal_volume

24

pub_type

杂志文章

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