Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation
about
Structural and functional insights into enzymes of the vitamin K cycleDetermination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Structural and functional analysis of cysteine residues in human glutamate decarboxylase 65 (GAD65) and GAD67.Chemical modification of cysteine residues is a misleading indicator of their status as active site residues in the vitamin K-dependent gamma-glutamyl carboxylation reaction.Nuclear alpha NAC influences bone matrix mineralization and osteoblast maturation in vivoTransmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase.gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates.Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiencyThe role of matrix gla protein in ossification and recovery of the avian growth plate.Extracellular matrix mineralization is regulated locally; different roles of two gla-containing proteins.Vitamin K oxygenation, glutamate carboxylation, and processivity: defining the three critical facets of catalysis by the vitamin K-dependent carboxylaseA new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry.Biochemical characterization of Drosophila gamma-glutamyl carboxylase and its role in fly development.r-VKORC1 expression in factor IX BHK cells increases the extent of factor IX carboxylation but is limited by saturation of another carboxylation component or by a shift in the rate-limiting step.Characteristics of recombinant W501S mutated human gamma-glutamyl carboxylase.Expression and characterization of recombinant vitamin K-dependent gamma-glutamyl carboxylase from an invertebrate, Conus textile.Identification of sequences within the gamma-carboxylase that represent a novel contact site with vitamin K-dependent proteins and that are required for activity.The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation.A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate.Truncated gamma-glutamyl carboxylase in rambouillet sheep.
P2860
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P2860
Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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2000年學術文章
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name
Identification of the vitamin ...... epoxidation and carboxylation
@en
Identification of the vitamin ...... epoxidation and carboxylation.
@nl
type
label
Identification of the vitamin ...... epoxidation and carboxylation
@en
Identification of the vitamin ...... epoxidation and carboxylation.
@nl
prefLabel
Identification of the vitamin ...... epoxidation and carboxylation
@en
Identification of the vitamin ...... epoxidation and carboxylation.
@nl
P2093
P2860
P356
P1476
Identification of the vitamin ...... epoxidation and carboxylation
@en
P2093
B N Pudota
K L Berkner
K S Misono
K W Hallgren
P2860
P304
13033-13038
P356
10.1073/PNAS.97.24.13033
P407
P577
2000-11-01T00:00:00Z