gamma-carboxyglutamic acid

γ-carboxyglutamic acid

/γ-car·boxy·glu·ta·mic ac·id/ (kahr-bok″se-gloo-tam´ik) an amino acid occurring in biologically active prothrombin, and formed in the liver in the presence of vitamin K by carboxylation of glutamic acid residues in prothrombin precursor molecules.
References in periodicals archive ?
9-Cis retinoio acid reduces 1 alpha,25-dihydroxycholecalciferol-induced renal calcification by altering vitamin K-dependent gamma-carboxylation of matrix gamma-carboxyglutamic acid protein in A/J male mice [abstract].
The name of this calcium-regulating protein is matrix gamma-carboxyglutamic acid.
Deteriorated calcium-dependent conformation of the gamma-carboxyglutamic acid domain relevant to a thrombotic tendency.
Vitamin K2 is a cofactor of gamma-carboxylase, which converts the glutamic acid (Glu) residue in osteocalcin molecules to gamma-carboxyglutamic acid (Gla), and is, therefore, essential for gamma-carboxylation of osteocalcin.
Osteocalcin (OC), a vitamin K-dependent protein expressed by osteoblasts, contains 3 gamma-carboxyglutamic acid residues derived from the vitamin K-dependent posttranslational modification of glutamic acid residues.
RESULTS: Vitamin K is required for the carboxylation of the amino acid glutamic acid to gamma-carboxyglutamic acids on proteins, which is essential for the calcium binding capacity of Gla proteins (such as osteocalcin).

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