A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate (Q44580839)

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scientific article published on 10 September 2003

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English	A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate	scientific article published on 10 September 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

4 December 2017

A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

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author name string

Vasantha P Mutucumarana

1

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Europe PubMed Central

PubMed publication ID

4 December 2017

Francine Acher

2

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4 December 2017

David L Straight

3

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4 December 2017

Da-Yun Jin

4

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4 December 2017

Darrel W Stafford

5

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4 December 2017

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publication date

10 September 2003

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4 December 2017

Journal of Biological Chemistry

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4 December 2017

278

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4 December 2017

47

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Europe PubMed Central

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4 December 2017

46488-46493

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Europe PubMed Central

PubMed publication ID

4 December 2017

Role of vitamin-K-dependent proteins in bone metabolism

1 reference

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The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade

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Primary structure and tissue distribution of two novel proline-rich γ-carboxyglutamic acid proteins

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Identification of two novel transmembrane gamma-carboxyglutamic acid proteins expressed broadly in fetal and adult tissues

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Vitamin K-dependent carboxylase: evidence for cofractionation of carboxylase and epoxidase activities, and for carboxylation of a high-molecular-weight microsomal protein

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Hereditary deficiency of all vitamin K-dependent procoagulants and anticoagulants

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Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase.

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Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase

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A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla

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On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila

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gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates

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Amino acids responsible for reduced affinities of vitamin K-dependent propeptides for the carboxylase

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21 January 2018

Cloning and Expression of the cDNA for Human γ-glutamyl Carboxylase

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A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase.

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Vitamin K-dependent carboxylase: influence of the "propeptide" region on enzyme activity

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In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells

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Cloning, structural organization, and transcriptional activity of the rat vitamin K-dependent gamma-glutamyl carboxylase gene

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Vitamin K and energy transduction: a base strength amplification mechanism

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Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation

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The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.

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21 January 2018

Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate

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21 January 2018

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

1 reference

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21 January 2018

Identification of sequences within the gamma-carboxylase that represent a novel contact site with vitamin K-dependent proteins and that are required for activity

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21 January 2018

Vitamin K-dependent carboxylase: effect of ammonium sulfate on substrate carboxylation and on inhibition by stereospecific substrate analogs

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21 January 2018

The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase

1 reference

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21 January 2018

Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase

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21 January 2018

The effect of S-warfarin administration on vitamin K 2,3-epoxide reductase activity in liver, kidney and testis of the rat

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21 January 2018

Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis

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21 January 2018

Synthesis of peptide analogues of prothrombin precursor sequence 5-9. Substrate specificity of vitamin K dependent carboxylase

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21 January 2018

Vitamin K-dependent carboxylase from calf liver: studies on the steady-state kinetic mechanism

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21 January 2018

The active site region of the vitamin K‐dependent carboxylase includes both the amino‐terminal hydrophobic and carboxy‐terminal hydrophilic domains of the protein

1 reference

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21 January 2018

Identification of the five hydrophilic residues (Lys-217, Lys-218, Arg-359, His-360, and Arg-513) essential for the structure and activity of vitamin K-dependent carboxylase

1 reference

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21 January 2018

Vitamin K dependent carboxylase: subcellular location of the carboxylase and enzymes involved in Vitamin K metabolism in rat liver

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21 January 2018

Identifiers

10.1074/JBC.M307707200

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

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