The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis. (Q35639926)

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scientific article published on 6 September 2011

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English	The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis.	scientific article published on 6 September 2011

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12 February 2020

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

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12 February 2020

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Kathleen L Berkner

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12 February 2020

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Mark A Rishavy

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12 February 2020

Kevin W Hallgren

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12 February 2020

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6 September 2011

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12 February 2020

Journal of Biological Chemistry

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12 February 2020

286

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12 February 2020

52

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12 February 2020

44821-44832

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Mutations in the GGCX and ABCC6 genes in a family with pseudoxanthoma elasticum-like phenotypes

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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

1 reference

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Vitamin K-dependent carboxylation

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Structure and function of vitamin K epoxide reductase

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Fatal hemorrhage in mice lacking gamma-glutamyl carboxylase

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Pseudoxanthoma elasticum-like phenotype with cutis laxa and multiple coagulation factor deficiency represents a separate genetic entity

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Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation

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Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiency

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The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation

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The vitamin K-dependent carboxylase

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A new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine

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Carboxylase overexpression effects full carboxylation but poor release and secretion of factor IX: implications for the release of vitamin K-dependent proteins

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Tethered processivity of the vitamin K-dependent carboxylase: factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo

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

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A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors

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Purification of vitamin K-dependent carboxylase from cultured cells

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Isolation of the human gamma-carboxylase and a gamma-carboxylase-associated protein from factor IX-expressing mammalian cells.

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Expression of recombinant vitamin K-dependent proteins in mammalian cells: factors IX and VII.

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Vitamin K and energy transduction: a base strength amplification mechanism

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The stereochemistry of hydrogen abstraction in vitamin K-dependent carboxylation

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

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Specific tritium labeling of .gamma.-carboxyglutamic acid in proteins

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Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors

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1 reference

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based on heuristic

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The inhibition of vitamin K-dependent carboxylase by cyanide

1 reference

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Vitamin K-dependent carboxylation. Study of the hydrogen abstraction stereochemistry with gamma-fluoroglutamic acid-containing peptides

1 reference

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Fate of the activated gamma-carbon-hydrogen bond in the uncoupled vitamin K-dependent gamma-glutamyl carboxylation reaction

1 reference

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Identifiers

10.1074/JBC.M111.249177

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21896484%20AND%20SRC:MED&resulttype=core&format=json

12 February 2020

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Europe PubMed Central

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12 February 2020

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Europe PubMed Central

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12 February 2020

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