Literature DB >> 1961725

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

P Dowd1, S W Ham.   

Abstract

Cyanide is a competitive inhibitor of carbon dioxide in the vitamin K-dependent glutamate carboxylase system, which plays a central role in the function of the blood clotting cascade. The mechanism of cyanide inhibition has been obscure for some time. At pH 7.2, cyanide (pKa = 9.21) will exist in solution as hydrogen cyanide to the extent of 99%. Hydrogen cyanide is linear triatomic molecule able to serve as a surrogate for carbon dioxide at the enzyme active site. Hydrogen cyanide is an acid; it will quench the deprotonated glutamate carbanion precursor to gamma-carboxyglutamate, resulting in inhibition of the carboxylation sequence.

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Year:  1991        PMID： 1961725      PMCID： PMC52973          DOI： 10.1073/pnas.88.23.10583

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  17 in total

1.  The interactions of acetoacetate decarboxylase with carbonyl compounds, hydrogen cyanide, and an organic mercurial.

Authors:  A P Autor; I Fridovich
Journal:  J Biol Chem       Date:  1970-10-25       Impact factor: 5.157

Review 2.  Vitamin K-dependent carboxylase.

Authors:  J W Suttie
Journal:  Annu Rev Biochem       Date:  1985       Impact factor: 23.643

Review 3.  Vitamin K-dependent carboxylation of glutamyl residues in proteins.

Authors:  J W Suttie
Journal:  Biofactors       Date:  1988-01       Impact factor: 6.113

4.  The inhibition of vitamin K-dependent carboxylase by cyanide.

Authors:  M De Metz; B A Soute; H C Hemker; C Vermeer
Journal:  FEBS Lett       Date:  1982-01-25       Impact factor: 4.124

Review 5.  The function and metabolism of vitamin K.

Authors:  R E Olson
Journal:  Annu Rev Nutr       Date:  1984       Impact factor: 11.848

6.  Vitamin K-dependent gamma-carbon-hydrogen bond cleavage and nonmandatory concurrent carboxylation of peptide-bound glutamic acid residues.

Authors:  P A Friedman; M A Shia; P M Gallop; A E Griep
Journal:  Proc Natl Acad Sci U S A       Date:  1979-07       Impact factor: 11.205

7.  Studies on the mechanism of the vitamin K-dependent carboxylation reaction. Carboxylation without the concurrent formation of vitamin K 2,3-epoxide.

Authors:  M de Metz; B A Soute; H C Hemker; R Fokkens; J Lugtenburg; C Vermeer
Journal:  J Biol Chem       Date:  1982-05-25       Impact factor: 5.157

8.  Vitamin K-dependent carboxylase. Stoichiometry of carboxylation and vitamin K 2,3-epoxide formation.

Authors:  A E Larson; P A Friedman; J W Suttie
Journal:  J Biol Chem       Date:  1981-11-10       Impact factor: 5.157

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

Authors:  J J McTigue; J W Suttie
Journal:  J Biol Chem       Date:  1983-10-25       Impact factor: 5.157

10.  Relationship between vitamin K-dependent carboxylation and vitamin K epoxidation.

Authors:  J W Suttie; A E Larson; L M Canfield; T L Carlisle
Journal:  Fed Proc       Date:  1978-10
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  2 in total

Review 1.  Vitamin K oxygenation, glutamate carboxylation, and processivity: defining the three critical facets of catalysis by the vitamin K-dependent carboxylase.

Authors:  Mark A Rishavy; Kathleen L Berkner
Journal:  Adv Nutr       Date:  2012-03-01       Impact factor: 8.701

2.  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
  2 in total

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