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  • Title: Vitamin K-dependent carboxylase. Solubilization and properties.
    Author: Esmon CT, Suttie JW.
    Journal: J Biol Chem; 1976 Oct 25; 251(20):6238-43. PubMed ID: 977568.
    Abstract:
    Vitamin K is required for an enzymatic carboxylation of glutamyl residues in a microsomal protein precursor of plasma prothrombin to form gamma-carboxyglutamic acid. The enzyme system (carboxylase) which catalyzes this reaction has now been solubilized by extraction of the microsomes with Triton X-100 and has been shown to fix H14CO3- as gamma-carboxyglutamic acid residues in biologically active prothrombin. Enzyme activity requires O2 and vitamin K hydroquinone or vitamin K + NADH. Unlike the microsomal-bound carboxylase, soluble carboxylase activity is independent of either ATP or Mg2+ addition and is unaffected by either the ATP analog, adenyl-5'-yl imidodiphosphate (AMP-P(NH)P, or EDTA. These observations suggest that the energy required to drive the carboxylation reaction is derived from the oxidation of the reduced form of vitamin K. Although the membrane-bound carboxylase is inhibited by Warfarin, this anticoagulant is ineffective as an inhibitor of the soluble enzyme. A second anticoagulant, 2-chloro-3-phytyl-1,4-natpthoquinone (chloro-K), differs from Warfarin in that it effectively inhibits both the membrane-bound and soluble carboxylases.
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