Literature DB >> 508335

Vitamin K-dependent carboxylation of synthetic substrates. Nature of the products.

P Decottignies-Le Maréchal, H Rikong-Aide, R Azerad, M Gaudry.   

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Year:  1979        PMID： 508335     DOI： 10.1016/0006-291x(79)91884-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  5 in total

1.  Functional Study of the Vitamin K Cycle Enzymes in Live Cells.

Authors:  J-K Tie; D W Stafford
Journal:  Methods Enzymol       Date:  2016-11-22       Impact factor: 1.600

Review 2.  Post-translational carboxylation of preprothrombin.

Authors:  B C Johnson
Journal:  Mol Cell Biochem       Date:  1981-08-11       Impact factor: 3.396

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
  5 in total

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