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

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

Item
http://www.wikidata.org/entity/Q44580839
Structural and functional insights into enzymes of the vitamin K cycleTransmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase.Mutations in the GGCX and ABCC6 genes in a family with pseudoxanthoma elasticum-like phenotypes.Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of {gamma}-glutamyl carboxylaseA hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis.Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders.Vitamin K oxygenation, glutamate carboxylation, and processivity: defining the three critical facets of catalysis by the vitamin K-dependent carboxylaseFamilial deficiency of vitamin K-dependent clotting factors.A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry.GGCX-Associated Phenotypes: An Overview in Search of Genotype-Phenotype Correlations.Methylation of γ-carboxylated Glu (Gla) allows detection by liquid chromatography-mass spectrometry and the identification of Gla residues in the γ-glutamyl carboxylase.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.The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation.
P2860

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

Item
http://www.wikidata.org/entity/Q44580839
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
A conserved region of human vi ...... with the glutamate substrate.
@en
A conserved region of human vi ...... with the glutamate substrate.
@nl
type
label
A conserved region of human vi ...... with the glutamate substrate.
@en
A conserved region of human vi ...... with the glutamate substrate.
@nl
prefLabel
A conserved region of human vi ...... with the glutamate substrate.
@en
A conserved region of human vi ...... with the glutamate substrate.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P356
P1433
P1476
A conserved region of human vi ...... with the glutamate substrate.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921