Literature DB >> 6138349

Vitamin K-dependent carboxylase. Demonstration of a vitamin K- and O2-dependent exchange of 3H from 3H2O into glutamic acid residues.

J J McTigue, J W Suttie.   

Abstract

The rat liver vitamin K-dependent carboxylase has been studied with t-butoxycarbonyl-Glu-Glu-Leu-OMe as a substrate. The crude enzyme preparation catalyzes incorporation of 3H from media 3H2O into the glutamic acid residues of the substrate. This incorporation is dependent on vitamin KH2 and O2, is stimulated by NaCN, and is inhibited by increasing the HCO3- concentration. These data lend support to an enzymatic mechanism involving a vitamin K- and O2-dependent formation of a carbanion at the gamma-position of the glutamic acid residue followed by attack of CO2 to form gamma-carboxyglutamic acid.

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Year:  1983        PMID: 6138349

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  6 in total

1.  Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state.

Authors:  I Sugiura; B Furie; C T Walsh; B C Furie
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-19       Impact factor: 11.205

Review 2.  Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase.

Authors:  C Vermeer
Journal:  Biochem J       Date:  1990-03-15       Impact factor: 3.857

3.  The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis.

Authors:  Mark A Rishavy; Kevin W Hallgren; Kathleen L Berkner
Journal:  J Biol Chem       Date:  2011-09-06       Impact factor: 5.157

4.  Vitamin K-dependent carboxylation. Mechanistic studies with 3-fluoroglutamate-containing substrates.

Authors:  A Vidal-Cros; M Gaudry; A Marquet
Journal:  Biochem J       Date:  1990-03-15       Impact factor: 3.857

5.  Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation.

Authors:  Mark A Rishavy; Kathleen L Berkner
Journal:  Biochemistry       Date:  2008-08-22       Impact factor: 3.162

6.  Mechanism of cyanide inhibition of the blood-clotting, vitamin K-dependent carboxylase.

Authors:  P Dowd; S W Ham
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-01       Impact factor: 11.205

  6 in total

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