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pubmed-article:2049381pubmed:abstractTextThe ability of des-gamma-carboxy bone Gla protein (dBGP) and des-gamma-carboxy matrix Gla protein (dMGP) to act as substrates for the rat liver vitamin K-dependent carboxylase has been investigated. An amino-terminal 'propeptide' is present on the intracellular form of BGP and is thought to interact with a recognition site on the enzyme. dBGP, lacking this extension, is a poor, high apparent Km, carboxylase substrate, but is a much better substrate when free propeptide is added. MGP lacks an amino-terminal propeptide, but contains a a homologous region in the mature protein. dMGP is an excellent substrate for the carboxylase with a low apparent Km and its carboxylation is inhibited by free propeptide.lld:pubmed
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pubmed-article:2049381pubmed:articleTitleVitamin K-dependent carboxylase: utilization of decarboxylated bone Gla protein and matrix Gla protein as substrates.lld:pubmed
pubmed-article:2049381pubmed:affiliationDepartment of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.lld:pubmed
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