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

Biochim Biophys Acta. 1991 May 30;1078(1):31-4. doi: 10.1016/0167-4838(91)90088-h.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / metabolism*
  • Carbon-Carbon Ligases*
  • Dansyl Compounds / metabolism
  • Decarboxylation
  • Extracellular Matrix Proteins*
  • In Vitro Techniques
  • Ligases / metabolism*
  • Male
  • Microsomes, Liver / enzymology
  • Molecular Sequence Data
  • Osteocalcin / metabolism*
  • Protein Precursors / metabolism
  • Rats
  • Substrate Specificity

Substances

  • Calcium-Binding Proteins
  • Dansyl Compounds
  • Extracellular Matrix Proteins
  • Protein Precursors
  • matrix Gla protein
  • Osteocalcin
  • 5-dimethylaminonaphthalene-1-sulfonamide
  • Ligases
  • Carbon-Carbon Ligases
  • glutamyl carboxylase