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Engelke, J.A. et al.

Vitamin K-dependent carboxylase: utilization of decarboxylated bone Gla protein and matrix Gla protein as substrates.

The 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.[1]

References

Vitamin K-dependent carboxylase: utilization of decarboxylated bone Gla protein and matrix Gla protein as substrates. Engelke, J.A., Hale, J.E., Suttie, J.W., Price, P.A. Biochim. Biophys. Acta (1991) [Pubmed]

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