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Information on EC 4.1.1.90 - peptidyl-glutamate 4-carboxylase
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4.1.1.90 peptidyl-glutamate 4-carboxylaseIUBMB Comments
The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron. The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system. 9--12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein. The 4-pro-S hydrogen of the glutamate residue is removed and there is an inversion of stereochemistry at this position .
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Word Map
- 4.1.1.90
- calcification
- co2
- ribulose
- biotin
- acetyl-coa
- phosphoenolpyruvate
- arterial
- ribulose-1,5-bisphosphate
- chloroplast
- rubisco
- warfarin
-
coagulation
- osteocalcin
- epoxide
-
bisphosphate
-
1,5-bisphosphate
-
propionyl
- spinach
-
gamma-carboxylation
- osteopontin
-
biotin-dependent
-
gamma-carboxyglutamic
-
4.1.1.39
- prothrombin
- propeptide
- rubp
-
calcify
- osteoprotegerin
- acidemia
- rhodospirillum
- biotinidase
- propionyl-coa
- rubrum
- rbcl
-
pepcs
- vkorc1
- fetuin-a
- accase
-
photorespiration
- osteonectin
- phylloquinone
-
crassulacean
-
pseudoxanthoma
-
undercarboxylated
- elasticum
- medicine
-
co2-fixing
- carboxysomes
- flaveria
- synthesis
-
carboxy-lyase
- phosphoribulokinase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
carboxylase, matrix gla protein, vitamin k-dependent carboxylase, gamma-glutamyl carboxylase, gamma-carboxylase, vitamin k-dependent gamma-glutamyl carboxylase, vkd carboxylase, vitamin k carboxylase, glutamate carboxylase, gamma glutamyl carboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gamma-glutamyl carboxylase
GGCX
glutamate carboxylase
matrix gamma-carboxyglutamate protein
matrix Gla protein
peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing)
-
-
two-chain carboxylase
-
carboxylase and epoxidase activities similar to those of one-chain carboxylase
vitamin K-dependent carboxylase
vitamin K-dependent gamma-glutamyl carboxylase
gamma-glutamyl carboxylase
-
-
glutamate carboxylase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinol
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinol
-
-
-
-
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinol
in the physiological process reaction runs in reversed direction
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
gamma-carboxylation
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing)
The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron. The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system. 9--12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein. The 4-pro-S hydrogen of the glutamate residue is removed [5] and there is an inversion of stereochemistry at this position [6].
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CAS REGISTRY NUMBER
COMMENTARY
81181-72-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
28-residue peptides based on residues -18 to +10 of human proprothrombin + CO2 + O2 + reduced vitamin K1
?
-
-
-
?
4-benzoyl-L-phenylalanine + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
BPA
-
-
?
CDADWVEGYSMEYLSR + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
CDADWVEGYSMEYLSR
-
-
?
CGRPSLEQLAQEVTYA + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
CGRPSLEQLAQEVTYA
-
-
?
conantokin G + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
poorly carboxylated
-
-
?
FLEEL + CO2 + O2 + ammonium sulfate
? + vitamin K epoxide + H2O
carboxylase activity is measured by 14CO2 incorporation into the synthetic peptide substrate FLEEL
-
-
?
FLEEL + CO2 + O2 + vitamin K1 hydroquinone
? + vitamin K1 epoxide + H2O
-
a synthetic peptide substrate, assay for vitamin Kdependent carboxylase activity
-
-
?
FLEEV + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
gamma-carboxylated glutamyl containing vitamin K-dependent protein + vitamin K epoxide + H2O
?
-
-
-
-
?
GKDRLTQMKRILKQRGNKARGEEELY + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
glutamyl containing vitamin K-dependent protein + CO2 + vitamin K hydroquinone + O2
?
-
propeptide binding increases carboxylase affinity for the Glu substrate, and the coordinated binding of the vitamin Kdependent propeptide and Glu substrate increase carboxylase affinity for vitamin K and activity, possibly through a mechanism of substrate-assisted catalysis. The propeptide adjacent to the Gla domain is cleaved subsequently to carboxylation. The carboxylase uses the energy of vitamin K hydroquinone oxygenation to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kdependent proteins. During carboxylation, the vitamin K hydroquinone cofactor is oxidized to a vitamin K epoxide product. The carboxylase itself is also a vitamin Kdependent protein and carboxylase carboxylation may be important in regulating the overall process of vitamin Kdependent protein carboxylation. All vitamin Kdependent proteins contain multiple glutamyl residues that undergo carboxylation, which is accomplished by a processive mechanism. A single binding event between carboxylase and vitamin Kdependent protein can give rise to all of the glutamyl to gamm-carboxylated glutamyl conversions in the vitamin Kdependent protein. Carboxylation is limited to the glutamyl residue residing within the Gla domain
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
N-(bromoacetyl)-FLEELY + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
-
-
-
?
osteocalcin + reduced vitamin K + CO2 + O2
? + vitamin K epoxide + H2O
-
-
-
?
osteocalcin + reduced vitamin K + CO2 + O2
carboxylated osteocalcin + vitamin K epoxide + H2O
-
-
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
peptidyl-L-glutamate + CO2 + O2 + phylloquinone
peptidyl-4-carboxy L-glutamate + 2,3-epoxyphylloquinone + H2O
-
-
-
-
?
precursor analog containing 12 of the propeptide region + CO2 + O2 + reduced vitamin K1
?
-
-
-
?
precursor analog containing 29 amino acids of the propeptide region + CO2 + O2 + reduced vitamin K1
?
-
-
-
?
pro-e-TxIX/12 + CO2 + O2 + vitamin KH2
?
residues -12 to -1 of e-TxIX precursor
-
-
?
pro-e-TxIX/24 + CO2 + O2 + vitamin KH2
?
residues -12 to +12 of e-TxIX precursor
-
-
?
pro-e-TxIX/41 + CO2 + O2 + vitamin KH2
?
residues -29 to +12 of e-TxIX precursor
-
-
?
pro-FIX19 + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
pro-FIX19: peptide comprising residues of human factor IX AVFLDHENANKILNRPKRY
-
-
?
pro-FIX19-16BPA + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
pro-FIX19-16BPA: peptide comprising residues TVBLDHENANKILNRPKRY
-
-
?
proFIX 19 + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
proFIX 19, peptide sequence: TVFLDHENANKILNRPKRY
-
-
?
ProFIX 19-6BPA + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
TVFLDHENANKIBNRPKR
-
-
?
ProFIX 19-7BPA + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
TVFLDHENfiNKBLNRPKR
-
-
?
proFIX/PT28 + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
proFIX/PT28, peptide sequence: TVFLDHENANKILNRPKRANTFLEEVRK
-
-
?
proFIX18 + CO2 + O2 + vitamin KH2
?
residues -18 to -1 of proFactor IX
-
-
?
proFIX19 + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
TVFLDHENANKILNRPKRY
-
-
?
ProFIX19-13BPA + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
TVFLDBENWKILNRPKRY
-
-
?
ProFIX19-16BPA + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
TVBLDHENANKILNRPKRY
-
-
?
proFIX28 + CO2 + O2 + vitamin KH2
?
residues -18 to +10 of proFactor IX
-
-
?
proFIXl9 + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
AVFLDHENANKILNRPKRY
-
-
?
proPT18 + CO2 + O2 + vitamin KH2
?
residues -18 to -1 of proprothrombin. 28-residue peptides based on residues -18 to +10 of human proprothrombin and proFactor IX with Km values of 420 lM, 1.7 microM and 6 microM
-
-
?
proPT28 + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
HVFLAPQQARSLLQRVRRANTFLEEVRK
-
-
?
proPT28 + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
proPT28: synthetic peptide is designated by the following nomenclature: pro indicates the presence of the propeptide sequence, PT indicates prothrombin, the protein on which the peptide sequence is based, and 28 indicates the number of amino acid residues in the peptide
-
-
?
proPT28 + CO2 + O2 + vitamin KH2
?
residues -18 to +10 of proprothrombin
-
-
?
proPTl8 + CO2 + O2 + FLEEL + vitamin KH2
? + vitamin K epoxide + H2O
HVFLAPQQARSLLQRVRR
-
-
?
TVFLDHENANKILNRPKRANTBLEEVRK + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
carboxylase probe1, TVFLDHENANKILNRPKRANTBLEEVRK as a substrate
-
-
?
TVFLDHENANKILNRPKRYNTBLEEVRK + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
YVFLDHQDADANLILNRPKR + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
-
-
-
?
FLEEL + CO2 + O2 + proFIX 19
? + vitamin K epoxide + H2O
carboxylase activity is measured by 14CO2 incorporation into the synthetic peptide substrate FLEEL
-
-
?
FLEEL + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
FLEEL + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
FLEEL + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
-
-
?
FLEEL + CO2 + O2 + vitamin K hydroquinone
? + vitamin K epoxide + H2O
-
pentapeptide substrate FLEEL: Phe-Leu-Glu-Glu-Leu, used for carboxylation activity
-
-
?
FLEEL + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
-
-
-
?
FLEEL + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
Phe-Leu-Glu-Glu-Leu
-
-
?
FLEEL + CO2 + O2 + vitamin KH2
? + vitamin K epoxide + H2O
carboxylase activity is measured by 14CO2 incorporation into the synthetic peptide substrate FLEEL
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
vitamin K epoxide must be recycled to vitamin K hydroquinone by the enzyme epoxide reductase for the reaction to continue
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
ir
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
the enzyme uses oxygenation of vitamin K hydroquinone to vitamin K epoxide to drive the incorporation of CO2 into glutamyl residues to produce carboxylated glutamate in vitamin K-dependent proteins
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
catalyzes modification of specific glutamic acids to gamma-carboxyglutamic acid in several blood-coagulation proteins
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
reaction is essential for the activity of all of the vitamin K-dependent proteins
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
-
-
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
-
-
-
-
?
additional information
?
-
enzyme catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxygutamic acid residues within the vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxygutamic acid residues within the vitamin K-dependent proteins
-
-
?
additional information
?
-
enzyme required for the posttranslational modification of vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme required for the posttranslational modification of vitamin K-dependent proteins
-
-
?
additional information
?
-
vitamin K-dependent carboxylation of glutamate to form gamma-carboxyglutamate (Gla) is unusual among known posttranslational modifications in that substrate recognition does not require a specific sequence around the glutamate residues to be modified
-
-
?
additional information
?
-
identification of a striking homology between exon 3 in all known matrix Gla proteins and a 24-residue sequence in the bovine and human gamma-glutamyl carboxylases. Alignment of exon 3 of matrix Gla protein with the homologous region of the gamma-glutamyl carboxylase shown
-
-
?
additional information
?
-
photolabeling of Q-glutamyl carboxylase with Bpa peptides
-
-
?
additional information
?
-
vitamin K carboxylase specifically interacts with the propeptide region of the precursor forms of vitamin K dependent proteins
-
-
?
additional information
?
-
amino-acid sequences of the synthetic substrates and propeptides are shown
-
-
?
additional information
?
-
-
amino-acid sequences of the synthetic substrates and propeptides are shown
-
-
?
additional information
?
-
one of the most distinctive of the extracellular post-translational modifications is the vitamin K-dependent gamma-carboxylation of glutamate residues to give gamma-carboxyglutamate
-
-
?
additional information
?
-
-
one of the most distinctive of the extracellular post-translational modifications is the vitamin K-dependent gamma-carboxylation of glutamate residues to give gamma-carboxyglutamate
-
-
?
additional information
?
-
enzyme accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins
-
-
?
additional information
?
-
enzyme important for gamma-carboxylation of gla-proteins
-
-
?
additional information
?
-
-
uses the oxygenation of vitamin K to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kdependent proteins
-
-
?
additional information
?
-
vitamin K-dependent carboxylation of glutamate to form gamma-carboxyglutamate (Gla) is unusual among known posttranslational modifications in that substrate recognition does not require a specific sequence around the glutamate residues to be modified
-
-
?
additional information
?
-
-
vitamin K-dependent proteins require carboxylation for activity
-
-
?
additional information
?
-
identification of a striking homology between exon 3 in all known matrix Gla proteins and a 24-residue sequence in the bovine and human gamma-glutamyl carboxylases. Alignment of exon 3 of matrix Gla protein with the homologous region of the gamma-glutamyl carboxylase shown
-
-
?
additional information
?
-
-
an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation
-
-
?
additional information
?
-
-
cis-isomer of vitamin K1, the 2-desmethyl derivative of phylloquinone, MK-1, or menadione (2 -methyl-1,4-naphthoquinone) have little or no activity
-
-
?
additional information
?
-
separate active sites are required to support vitamin K-dependent epoxide formation and carboxylation. The binding site for vitamin K oxygenase contains an active thiol group
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy-L-glutamate + vitamin K epoxide + H2O
-
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
peptidyl-L-glutamate + CO2 + O2 + phylloquinone
peptidyl-4-carboxy L-glutamate + 2,3-epoxyphylloquinone + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
-
?
L-glutamate + CO2 + O2 + vitamin K hydroquinone
gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
-
-
-
-
?
peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O
peptidyl-glutamate + CO2 + O2 + phylloquinone
-
-
-
-
?
additional information
?
-
enzyme catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxygutamic acid residues within the vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxygutamic acid residues within the vitamin K-dependent proteins
-
-
?
additional information
?
-
enzyme required for the posttranslational modification of vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme required for the posttranslational modification of vitamin K-dependent proteins
-
-
?
additional information
?
-
vitamin K-dependent carboxylation of glutamate to form gamma-carboxyglutamate (Gla) is unusual among known posttranslational modifications in that substrate recognition does not require a specific sequence around the glutamate residues to be modified
-
-
?
additional information
?
-
one of the most distinctive of the extracellular post-translational modifications is the vitamin K-dependent gamma-carboxylation of glutamate residues to give gamma-carboxyglutamate
-
-
?
additional information
?
-
-
one of the most distinctive of the extracellular post-translational modifications is the vitamin K-dependent gamma-carboxylation of glutamate residues to give gamma-carboxyglutamate
-
-
?
additional information
?
-
enzyme accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins
-
-
?
additional information
?
-
-
enzyme accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins
-
-
?
additional information
?
-
enzyme important for gamma-carboxylation of gla-proteins
-
-
?
additional information
?
-
-
uses the oxygenation of vitamin K to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kdependent proteins
-
-
?
additional information
?
-
vitamin K-dependent carboxylation of glutamate to form gamma-carboxyglutamate (Gla) is unusual among known posttranslational modifications in that substrate recognition does not require a specific sequence around the glutamate residues to be modified
-
-
?
additional information
?
-
-
vitamin K-dependent proteins require carboxylation for activity
-
-
?
additional information
?
-
-
an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation
-
-
?
additional information
?
-
-
cis-isomer of vitamin K1, the 2-desmethyl derivative of phylloquinone, MK-1, or menadione (2 -methyl-1,4-naphthoquinone) have little or no activity
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
menadione does not work as a cofactor for gamma-glutamylcarboxylase
-
vitamin K
carboxylase and soybean seed lipoxygenase share 19.3% identity over a span of 198 amino acids, from residues 468 to 666 of carboxylase. This is interesting because the carboxylase acts as an oxygenase on the cofactor vitamin K-hydroquinone, and the similarity occurs in that region of the carboxylase likely to have enzymatic function
vitamin K
conversion of glutamic acid to gamma-carboxyglutamic acid is coupled with the oxygenation of KH2 to vitamin K 2,3-epoxide and has been referred to as vitamin K epoxidase activity
vitamin K
-
the carboxylase uses the energy of vitamin K hydroquinone oxygenation to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kdependent proteins. During carboxylation, the vitamin K hydroquinone cofactor is oxidized to a vitamin K epoxide product
vitamin K
-
the enzyme requires vitamin K as a cofactor for its post-translational modification of glutamic acid residues to gamma-carboxyglutamic acid residues
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Mn2+, high concentrations significantly decrease or have no effect on Km of a peptide substrate for the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,5,6-Tetrachloro-4-pyridinol
-
TCP, anticoagulant action, effective in vitro inhibitor of the carboxylase
anti-carboxylase antiserum
effect of anti-carboxylase antiserum on carboxylase activity: under the conditions employed the carboxylation is inhibited by 80%, with parallel inhibition of CO2 incorporation into FLEEL and proPT28 (synthetic peptide)
-
Boc-(2S,4S)-4-methylglutamic acid-Glu-Val
competitive inhibitor, FLEEL as substrate
Boc-Ser(OPO4)-Ser(OPO4)-Leu-OMe
-
inhibits the enzyme apparently competitively with regard to other peptide substrate
bromoacetyl-FLEEL peptide
the His6-carboxylase is irreversibly inactivated. Up to 85% of the carboxylase activity is lost over a period of 120 min
FLEEL
-
high FLEEL peptide substrate concentrations (from 1.2 up to 12 mM) inhibit GGCX activity
p-chloromercuribenzoate
97% inhibition with 1.25 mM and at 5 mM the reaction is completely inhibited
proFIX/PT28 (Bpa +4)
presence of proFIX/PT28 (Bpa +4) or its iodinated derivative 56% inactivation is observed
-
protease inhibitor mixture
PIC, freshly prepared as a 10x PIC stock containing 20 mM dithiothreitol, 20 mM EDTA, FFRCK (1.25 microg/ml), FPRCK (1.25 microg/ml), leupeptin (5 microg/ml), pepstatin A (7 microg/ml), phenylmethylsulfonyl fluoride (340 microg/ml), aprotinin (20 microg/ml)
-
TVFLDHENANKILNRPKRANTBLEEVRK
the enzyme is photoirradiated on ice at 365 nm with TVFLDHENANKILNRPKRANTBLEEVRK, TVFLDHENANKILNRPKRYNTBLEEVRK and mono [127I]TVFLDHENANKILNRPKRYNTBLEEVRK for various times
TVFLDHENANKILNRPKRYNTBLEEVRK
the enzyme is photoirradiated on ice at 365 nm with TVFLDHENANKILNRPKRANTBLEEVRK, TVFLDHENANKILNRPKRYNTBLEEVRK and mono [127I]TVFLDHENANKILNRPKRYNTBLEEVRK for various times. Presence of TVFLDHENANKILNRPKRYNTBLEEVRK or its iodinated derivative 80% inactivation is observed
vitamin K
carboxylation of FLEEL by bovine liver carboxylase is inhibited by high concentrations of vitamin KH2. vitamin K (up to 400 mM) and vitamin K epoxide (up to 1 mM) are not inhibitory. R234A/H235A mutant, R406A/H408A mutant, and R513A/K515A mutant are more susceptible to inhibition by vitamin KH2 than wild type enzyme. R234A/H235A mutant and R406A/H408A mutant exhibit maximal activity at 111 mM vitamin KH2 and R513A/K515A mutant at 56 mM vitamin KH2
2-chloro-3-phytyl-1,4-naphthoquinone
-
chloro-K, effective in vivo antagonist of vitamin K, inhibits the enzyme in an competitive fashion
N-ethylmaleimide
preincubation with vitamin K hydroquinone prevents NEM inhibition of epoxide formation but not of carboxylation
p-hydroxymercuribenzoate
1 mM, more than 90% inhibition, inhibition is reversed by dithiothreitol
additional information
in the presence of high concentrations of propeptide, only minimal carboxylase activity is measurable. Antibodies to the protein inhibit the carboxylase activity in crude preparations
-
additional information
-
in the presence of high concentrations of propeptide, only minimal carboxylase activity is measurable. Antibodies to the protein inhibit the carboxylase activity in crude preparations
-
additional information
15 min irradiation in the absence of peptide resulted in a 10% inactivation of the carboxylase
-
additional information
-
the carboxylase reaction is inhibited by sulfhydryl-specific reagents
-
additional information
NADH, dithiothreitol, and ATP deficiency decrease enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzoylphenylalanine
Bpa, the four Bpa peptides enhance gamma-carboxylation by 1.5-2.3fold, and the rate enhancement profiles are very similar to that of proFIX19, showing that these propeptides are recognized by the carboxylase
FLEEL
-
the enzyme activity increases with increasing FLEEL peptide concentration up to 1.2 mM
N-ethyl-2-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)hexadecylamide
-
2fold higher carboxylated osteocalcin synthesis in MG-63 cells in presence of the compound than with menaquinone-4. No cytotoxicity observed with concentrations up to 500 nM
proFIX19
enhances gamma-carboxylation of the synthetic FLEEL peptide by 2.2-2.3fold
proPT18
enhances gamma-carboxylation of the synthetic FLEEL peptide by 2.2-2.3fold
-
additional information
-
enzyme activity increases 2-3fold by a vitamin K deficiency or Warfarin treatment
-
N-ethyl-2-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)tetradecylamide
-
2.5fold higher carboxylated osteocalcin synthesis in MG-63 cells in presence of the compound than with menaquinone-4, No cytotoxicity observed with concentrations up to 500 nM
N-ethyl-2-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)tetradecylamide
-
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
28-residue peptides based on residues -18 to +10 of human proprothrombin
pH 7.0
-
0.074
precursor analog containing 29 amino acids of the propeptide region
pH 7.0
-
0.0068
TVFLDHENANKILNRPKRANTBLEEVRK
carboxylase probe1, TVFLDHENANKILNRPKRANTBLEEVRK as a substrate
additional information
additional information
Km-values measured by hyperbolic weighted least-squares analysis
-
1.5
FLEEL
for wild type FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.004
vitamin KH2
proPT28, FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.074
vitamin KH2
FLEEL, FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.0023
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.78
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
0.78
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 160 microM
0.91
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
0.92
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 160 microM
1.01
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, proIX18 concentration 160 microM
1.23
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
1.25
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
1.54
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
1.78
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
2.01
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
2.03
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
2.06
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
FLEEL
for wild type FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.02
vitamin KH2
proPT28, FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.66
vitamin KH2
FLEEL, FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.01
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
0.015
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
0.02
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase
0.059
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM
0.153
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
0.175
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
0.324
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0.16 microM
0.347
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
0.391
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
0.465
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 1.6 microM
0.488
YVFLDHQDADANLILNRPKR
FLAG-vitamin K-dependent gamma-glutamyl carboxylase, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 160 microM
0.56
YVFLDHQDADANLILNRPKR
R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 160 microM
0.645
YVFLDHQDADANLILNRPKR
R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 160 microM
additional information
additional information
kcat values relative to wild type are 51% (L394R), 1% (Y395A), and 2% (W399A), pH 7.4, 20°C
-
additional information
additional information
-
kcat values relative to wild type are 51% (L394R), 1% (Y395A), and 2% (W399A), pH 7.4, 20°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0174
proFIX19-16BPA propeptide
competitive inhibition experiments using prom28 substrate
-
additional information
additional information
Ki value for Boc-(2S,4S)-4-methylglutamic acid-Glu-Val is above 5 mM for W399A, pH 7.4, 20°C
-
additional information
additional information
-
Ki value for Boc-(2S,4S)-4-methylglutamic acid-Glu-Val is above 5 mM for W399A, pH 7.4, 20°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
propeptide eluate of gel: 608 U/mg, carboxylase units are expressed as 100000 dpm of 14CO2 fixed in the standard assay
additional information
-
propeptide eluate of gel: 608 U/mg, carboxylase units are expressed as 100000 dpm of 14CO2 fixed in the standard assay
additional information
specific activities of the partially purified microsomes and the homogeneous vitamin K-dependent carboxylase are 2.77 and 279.6 nmol of vitamin K epoxide per h per mg of protein, a 101fold purification of the vitamin K epoxidase activity from partially purified microsomes
additional information
-
specific activities of the partially purified microsomes and the homogeneous vitamin K-dependent carboxylase are 2.77 and 279.6 nmol of vitamin K epoxide per h per mg of protein, a 101fold purification of the vitamin K epoxidase activity from partially purified microsomes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.4
-
assay at. The activity falls off sharply above pH 8 or below pH 7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
schematic of amino acid homology between human and the Drosophila gamma-glutamyl carboxylase shown
UniProt
brenda
Wistar strain male albino rats, vitamin K-deficient or warfarin-treated
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
vitamin K-dependent carboxylase mRNA expression in early rat embryonic development
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
expression of rat vitamin K-dependent carboxylase in adult and embryonic tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
human glutamyl carboxylase spans the membrane at least 5times, with its N-terminus in the cytoplasm and its C-terminus in the lumen of the endoplasmic reticulum
brenda
-
potential impact of quality control components on carboxylation, which occurs in the endoplasmic reticulum during the secretion of vitamin Kdependent proteins
brenda
amino-terminus of the gamma-glutamyl carboxylase is on the cytoplasmic side of the endoplasmic reticulum, while the carboxylterminus is on the lumenal side
brenda
microsomal carboxylase activity is compared from cells transfected with pCMV5
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
onset of mineralization in Abcc6-/-, Ggcx+/+ mice is delayed until between 3 and 4 months of age, suggesting that the genetic background plays a role in modifying the mineralization process. Mineralization in the Abcc6-/-, Ggcx+/- mice is accelerated in comparison with age-matched Abcc6-/-, Ggcx+/+ mice, with ca. 3fold difference at 3, 4, and 9 months of age
physiological function
physiological function
-
functional GGCX mutations in all 15 exons do not occur in most calcium oxalate urolithiasis patients, thus no significant association between the low activity and mutation of GGCX in calcium oxalate urolithiasis
physiological function
-
genetic variation in GGCX influences the gamma carboxylation of vitamin K-dependent proteins, as measured by differences in percent undercarboxylated osteocalcin and proteins induced by vitamin K absence-factor II (PIVKA-II). Heterozygous carriers of GGCX rs10187424 and rs7568458 have significantly lower percent undercarboxylated osteocalcin relative to either homozygous group. No significant differences within GGCX genotype group for plasma phylloquinone. No significant associations of GGCX polymorphisms and PIVKA-II
physiological function
-
genetic variations in GGCX gene contributes to impaired metabolism of warfarin
physiological function
-
GGCX mutations cause coagulation disorder and pseudoxanthoma elasticum. Two GGCX mutations from affected individuals (p. R83W and p.Q374X). GGCX is necessary for activation of both coagulation factors in the liver and matrix gla protein, which, in fully carboxylated form, is able to prevent ectopic mineralization
physiological function
-
relevance between the defect of GGCX and urolithasis. Decreased activity and production of GGCX between calcium oxalate urolithiasis patients and control patients. GGCX may play an important role in the formation of calcium oxalate. The decreased expression of GGCX may lead to the defect of activity, and may result in the declined ability of calcium oxalate of urinary prothrombin fragment 1
physiological function
-
two novel splice site mutations in the GGCX gene, G to T transversion of the first nucleotide of intron 2 (c. 1358+1G-T) and an A to G transversion of the third nucleotide of intron 11 (c. 10363+3A-G)
physiological function
VKC maintains vitamin K levels and sustains the blood coagulation cascade
physiological function
-
characterization of specific domains of GGCX that exhibit structural rearrangements upon binding the high-affinity consensus propeptide pCon (AVFLSREQANQVLQRRRR). pCon binding is specific for monomeric GGCX-nanodiscs and promotes enhanced structural stability to the nanodisc-integrated complex while maintaining catalytic activity in the presence of carboxylation cosubstrates. Modifications in hydrogen exchange of GGCX are prominently observed in GGCX peptides 491-507 and 395-401 upon pCon association, consistent with sites for propeptide and glutamate binding
physiological function
GGCX expressed in osteoblasts is critical for the maintenance of blood glucose and white adipose tissue. Osteoblast-specific conditional Ggcx-deficient mice exhibit altered metabolism compared with their controls. Serum glucose levels can be maintained with low amounts of insulin, and the weight of white adipose tissue significantly decreases
Show AA Sequence and Transmembrane Helices (805 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
SDS-PAGE, Sf21 cells transfected with the carboxylase cDNA-containing plasmid, Western Blot
60000
proteinase K digestion of the hGC-FLAG reveals a 60 kDa fragment, indicating the lumenal location of the FLAG tag and therefore the carboxyl-terminus of the carboxylase. In contrast, FLAG-hGC does not show a proteinase Kresistant fragment except for the residual undigested full-length carboxylase, which indicates the cytoplasmic location of the FLAG tag and therefore the amino-terminus of the carboxylase
77000
single major band on SDS gel electrophoresis. The eluted protein contains both stable vitamin K-dependent carboxylase and vitamin K epoxidase activity
94000
99000
SDS-PAGE, Western Blot. CHO cells transfected with the cDNA for wild type FLAG-vitamin K-dependent gamma-glutamyl carboxylase
additional information
-
determination of disulfide bond formation in purified two-chain carboxylase and P80L and P378L two-chain carboxylases by SDS-PAGE and Western Blot analyses
94000
SDS-PAGE and Western Blot, His6-carboxylase-Ac-FLEEL confirming affinity-purified carboxylase
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
binding site in the carboxyl half of the gamma-glutamyl carboxylase. Carboxylase may be cleaved by trypsin into an amino-terminal 30 kDa and a carboxyl-terminal 60 kDa fragment joined by disulfide bond(s), and the propeptide binds to the 60 kDa fragment
additional information
-
binding site in the carboxyl half of the gamma-glutamyl carboxylase. Carboxylase may be cleaved by trypsin into an amino-terminal 30 kDa and a carboxyl-terminal 60 kDa fragment joined by disulfide bond(s), and the propeptide binds to the 60 kDa fragment
additional information
limited tryptic digestion of the carboxylase yields two disulfide-linked fragments with molecular masses of 30 and 60 kDa, corresponding to the amino and carboxy-terminal part of the gamma-glutamyl carboxylase
additional information
-
disulfide bond between cysteines 99 and 450, five transmembrane domains
additional information
-
five transmembrane domains. Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme catalyzes vitamin K-dependent posttranslational modification of glutamate to gamma-carboxyl glutamate
additional information
-
enzyme catalyzes vitamin K-dependent posttranslational modification of glutamate to gamma-carboxyl glutamate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R234A/H235A
vitamin K epoxidase activities are reduced in parallel with the carboxylase activities. Showed defects in the propeptide binding site. Slightly faster mobility than wild-type FLAG-CBX. CBX234/235
R359A/H360A/K361A
vitamin K epoxidase activities are reduced in parallel with the carboxylase activities. Showed defects in the propeptide binding site. CBX359/360/361
R406A/H408A
vitamin K epoxidase activities are reduced in parallel with the carboxylase activities. Showed defects in the propeptide binding site. CBX406/408
R513A/K515A
vitamin K epoxidase activities are reduced in parallel with the carboxylase activities. The show normal affinity for the propeptide, FLEEL, proPT28, and vitamin K hydroquinone but exhibited a low catalytic rate for carboxylation. CBX513/515
E373L/Q374L
-
transmembrane domain residues in the C-terminal peptide to test for polar/charge residues
G363L/T367L
-
transmembrane domain residues in the C-terminal peptide to test for polar/charge residues
H404A
carboxylases W390A, S398A, and H404A have activities similar to that of wild type
K218A
-
K218A activity is not detectable. The addition of exogenous amines restores K218A activity while having little effect on wild type carboxylase
L394R
natural mutant, certain individuals with combined deficiencies of vitamin K-dependent proteins have a mutation, L394R, in their gamma-glutamyl carboxylase causing impaired glutamate binding
P80L
-
mutation of residue P80, which has activity similar to that of wild-type carboxylase, has a minor effect on disulfide formation
S398A
carboxylases W390A, S398A, and H404A have activities similar to that of wild type
W390A
carboxylases W390A, S398A, and H404A have activities similar to that of wild type
additional information
additional information
R234A/H235A mutant, R406A/H408A mutant, and R513A/K515A mutant are more susceptible to inhibition by vitamin KH2 than wild type enzyme. R234A/H235A mutant and R406A/H408A mutant exhibit maximal activity at 111 mM vitamin KH2 and R513A/K515A mutant at 56 mM vitamin KH2
additional information
-
R234A/H235A mutant, R406A/H408A mutant, and R513A/K515A mutant are more susceptible to inhibition by vitamin KH2 than wild type enzyme. R234A/H235A mutant and R406A/H408A mutant exhibit maximal activity at 111 mM vitamin KH2 and R513A/K515A mutant at 56 mM vitamin KH2
additional information
38-BamHI site introduces 2 amino acid residues (glycine and serine) between the hGC fragment and the Lep tag. A 10-amino acid peptide (MDYKDDDDKG), including the FLAG epitope, is introduced to the amino-terminus of the full length of hGC to make FLAG-hGC and a 8-amino acid peptide (DYKDDDDK) is attached to the carboxyl-terminus of the full length of hGC to make hGC-FLAG. The FLAG-tagged hGC cDNA is subcloned into the EcoRI (Escherichia coli RY13) site of the expression vector pCl-neo under control of the cytomegalovirus (CMV) promoter
additional information
-
38-BamHI site introduces 2 amino acid residues (glycine and serine) between the hGC fragment and the Lep tag. A 10-amino acid peptide (MDYKDDDDKG), including the FLAG epitope, is introduced to the amino-terminus of the full length of hGC to make FLAG-hGC and a 8-amino acid peptide (DYKDDDDK) is attached to the carboxyl-terminus of the full length of hGC to make hGC-FLAG. The FLAG-tagged hGC cDNA is subcloned into the EcoRI (Escherichia coli RY13) site of the expression vector pCl-neo under control of the cytomegalovirus (CMV) promoter
additional information
-
N-terminal carboxylase peptide (residues 1-345) and the C-terminal peptide (345-758) two-chain form (residues 1-345 and residues 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase expressed in Sf9 insect cells. The carboxylase and epoxidase activities similar to those of one-chain carboxylase. The two-chain carboxylase is joined by a disulfide bond
additional information
six out of seven patients with Pseudoxanthoma Elasticum habor mutations in the GGCX gene (gamma-glutamyl carboxylase)
additional information
Y395A propeptide affinity is similar to that of wild type, but those of L394R and W399A are 16-22fold less than that of wild type. Results of kinetic studies with a propeptide-containing substrate are consistent with results of propeptide binding and FLEEL kinetics. Although propeptide and vitamin K binding in some mutants are affected, our data provide compelling evidence that glutamate recognition is the primary function of the conserved region around Leu394
additional information
-
Y395A propeptide affinity is similar to that of wild type, but those of L394R and W399A are 16-22fold less than that of wild type. Results of kinetic studies with a propeptide-containing substrate are consistent with results of propeptide binding and FLEEL kinetics. Although propeptide and vitamin K binding in some mutants are affected, our data provide compelling evidence that glutamate recognition is the primary function of the conserved region around Leu394
additional information
-
GGCX single nucleotide polymorphism rs11676382(but not rs12714145) is a significant predictor of residual warfarin dosing error and is associated with a 6.1% reduction in warfarin dose per G allele
additional information
-
analysis of a Ggcx+/- intercross reveals a partial developmental block with only 50% of expected Ggcx-/- offspring surviving to term, with the latter animals dying uniformly at birth of massive intra-abdominal hemorrhage. This phenotype closely resembles the partial midembryonic loss and postnatal hemorrhage previously reported for both prothrombin and factor V (F5)deficient mice. Ggcx-/-, dying uniformly at birth of massive intra-abdominal hemorrhage. Heterozygous mice carrying a null mutation at the gamma-carboxylase (Ggcx) gene exhibit normal development and survival with no evidence of hemorrhage and normal functional activity of the vitamin Kdependent clotting factors IX, X, and prothrombin
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
enzyme is not very stable at 37°C and lower temperatures are more desirable. At temperatures below 20°C, extended linear rates of incorporation of 14CO2 into exogenous peptide substrates can be observed
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
degree of purification is about 7000fold with reference to ammonium sulfate-fractionated microsomal protein from liver. Purification of carboxylase, solubilized microsomes: 281000 cpm/mg/h, flow-through of Affi-FIXQ/S: 200000 cpm/mg/h, bound to Affi-FIXQ/S: 140000000 cpm/mg/h, affinity-purified carboxylase: 1930000000 cpm/mg/h
inactivated His6-carboxylase-Ac-FLEEL purified under denaturing conditions by Ni-chelation chromatography followed by preparative polyacrylamide gel electrophoresis
partial purification of the enzyme by antibody affinity techniques. Purified 500fold by adsorption to an antiprothrombin column and elution with a dodeca peptide which competes with a prothrombin precursor enzyme recognition site. The purified enzyme is devoid of bound precursors, and has the same ratio of vitamin K epoxidase activity to carboxylase activity as the crude microsomal preparation
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in baculovirus-infected insect cell. Produced His6-tagged carboxylase as a recombinant protein using a baculovirus expression system
expressed in Chinese hamster ovary cells with an immunodetectable octapeptide inserted at the amino-terminal ends
expression of the cloned cDNA results in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells
His6-tagged bovine liver carboxylase (His6-carboxylase) is produced in insect cells using a baculovirus expression system
mutational analysis is performed using an expression system lacking endogenous carboxylase. Construction of baculo viruses containing FLAG-tagged carboxylase mutants and expression in infected SF21 cells. Expresses the 758 amino acid human VKD carboxylase bearing a C-terminal extension of AAADYKDDDDK, where the last eight amino acids are the FLAG epitope
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GGCX mRNA in the urolithiasic group is lower than that in the normal control group, which is on average 7.86fold underexpressed in the urolithiasic group compared to the normal control group. Protein expression of GGCX in the urolithiasic group is weaker than that in the control groups
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
-
development of expression vectors which enable expressing mammalian gamma-glutamyl carboxylase, vitamin K epoxide reductase complex, subunit 1, and/or PDIA2 along with human coagulation factor VII in Drosophila Schnieder S2 cells. Mammalian GGCX i indispensable to synthesize active factor VII while mammalian vitamin K epoxide reductase complex, subunit 1, and PDIA2 are not critical but supportive factors for S2 cells
medicine
six out of seven patients with Pseudoxanthoma Elasticum habor mutations in the GGCX gene (gamma-glutamyl carboxylase)
medicine
-
multiplexed single nucleotide polymorphism panel (interrogation of the CYP2C9 *2, *3, VKORC1 (-1639G3A), and GGCX (1181T3G) alleles simultaneously) can be successfully used in genotyping of patient blood samples, whereby results can be combined with other clinical parameters in an algorithm for warfarin dosing
medicine
-
single nucleotide polymorphism in the GGCX gene may affect the dose of warfarin and other vitamin K antagonists
medicine
-
in WKY rats receiving a vitamin K-deficient diet that results in a 40% decrease of prothrombin activity, compound N-ethyl-2-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)tetradecylamide is able to counteract the effects on vitamin K deficiency and results in the complete restoration of prothrombin activity
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Bos taurus (Q07175), Bos taurus
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Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.
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Rishavy, M.A.; Hallgren, K.W.; Yakubenko, A.V.; Shtofman, R.L.; Runge, K.W.; Berkner, K.L.
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Rattus norvegicus (O88496)
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Romero, E.E.; Deo, R.; Velazquez-Estades, L.J.; Roth, D.A.
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248
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Rattus norvegicus (O88496)
brenda
Yamada, M.; Kuliopulos, A.; Nelson, N.P.; Roth, D.A.; Furie, B.; Furie, B.C.; Walsh, C.T.
Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators: carboxylase using benzoylphenylalanine photoaffinity peptide inactivators
Biochemistry
34
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1995
Bos taurus (Q07175)
brenda
Tie, J.K.; Zheng, M.Y.; Hsiao, K.L.; Perera, L.; Stafford, D.W.; Straight, D.L.
Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase
Biochemistry
47
6301-6310
2008
Homo sapiens
brenda
Helgeland, L.
The submicrosomal site for the conversion of prothrombin precursor to biologically active prothrombin in rat liver
Biochim. Biophys. Acta
499
181-193
1977
Rattus norvegicus (O88496)
brenda
Zhu, A.; Sun, H.; Raymond, R.M. Jr.; Furie, B.C.; Furie, B.; Bronstein, M.; Kaufman, R.J.; Westrick, R.; Ginsburg, D.
Fatal hemorrhage in mice lacking (gamma)-glutamyl carboxylase
Blood
109
5270-5275
2007
Mus musculus
brenda
Tie, J.; Wu, S.; Jin, D.; Nicchitta, C.V.; Stafford, D.W.
A topological study of the human gamma-glutamyl carboxylase
Blood
96
973-978
2000
Homo sapiens (P38435), Homo sapiens
brenda
Czerwiec, E.; Begley, G.S.; Bronstein, M.; Stenflo, J.; Taylor, K.; Furie, B.C.; Furie, B.
Expression and characterization of recombinant vitamin K-dependent gamma-glutamyl carboxylase from an invertebrate, Conus textile
Eur. J. Biochem.
269
6162-6172
2002
Conus textile (Q8IA33), Conus textile
brenda
Romero, E.E.; Velazquez-Estades, L.J.; Deo, R.; Schapiro, B.; Roth, D.A.
Cloning of rat vitamin K-dependent gamma-glutamyl carboxylase and developmentally regulated gene expression in postimplantation embryos
Exp. Cell Res.
243
334-346
1998
Rattus norvegicus (O88496)
brenda
Maillet, M.; Morris, D.; Gaudry, M.; Marquet, A.
The active site region of the vitamin K-dependent carboxylase includes both the amino-terminal hydrophobic and carboxy-terminal hydrophilic domains of the protein
FEBS Lett.
413
1-6
1997
Bos taurus (Q07175)
brenda
Morris, D.P.; Soute, B.A.; Vermeer, C.; Stafford, D.W.
Characterization of the purified vitamin K-dependent gamma-glutamyl carboxylase
J. Biol. Chem.
268
8735-8742
1993
Bos taurus (Q07175), Bos taurus
brenda
Kuliopulos, A.; Nelson, N.P.; Yamada, M.; Walsh, C.T.; Furie, B.; Furie, B.C.; Roth, D.A.
Localization of the affinity peptide-substrate inactivator site on recombinant vitamin K-dependent carboxylase
J. Biol. Chem.
269
21364-21370
1994
Bos taurus (Q07175), Bos taurus
brenda
Wu, S.M.; Mutucumarana. V.P.; Geromanos, S.; Stafford, D.W.
The propeptide binding site of the bovine gamma-glutamyl carboxylase
J. Biol. Chem.
272
11718-11722
1997
Bos taurus (Q07175), Bos taurus
brenda
Walker, C.S.; Shetty, R.P.; Clark, K.; Kazuko, S.G.; Letsou, A.; Olivera, B.M.; Bandyopadhyay, P.K.
On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila
J. Biol. Chem.
276
7769-7774
2001
Drosophila melanogaster (Q9W0C4), Drosophila melanogaster
brenda
Mutucumarana, V.P.; Acher, F.; Straight, D.L.; Jin, D.Y.; Stafford, D.W.
A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate
J. Biol. Chem.
278
46488-46493
2003
Homo sapiens (P38435), Homo sapiens
brenda
Vanakker, O.M.; Martin, L.; Gheduzzi, D.; Leroy, B.P.; Loeys, B.L.; Guerci, V.I.; Matthys, D; Terry, S.F.; Coucke, P.J.; Pasquali-Ronchetti, I.; De Paepe, A.
Pseudoxanthoma elasticum-like phenotype with cutis laxa and multiple coagulation factor deficiency represents a separate genetic entity
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127
581-587
2007
Homo sapiens (P38435)
brenda
Crosier, M.D.; Peter, I.; Booth, S.L.; Bennett, G.; Dawson-Hughes, B.; Ordovas, J.M.
Association of sequence variations in vitamin K epoxide reductase and gamma-glutamyl carboxylase genes with biochemical measures of vitamin K status
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55
112-119
2009
Homo sapiens
brenda
Stafford, D.W.
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3
1873-1878
2005
Homo sapiens
brenda
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Vitamin K-dependent proteins in Ciona intestinalis, a basal chordate lacking a blood coagulation cascade
Proc. Natl. Acad. Sci. USA
103
15794-15799
2006
Ciona intestinalis (Q008V9), Ciona intestinalis
brenda
Wu, S.M.; Morris, D.P.; Stafford, D.W.
Identification and purification to near homogeneity of the vitamin K-dependent carboxylase
Proc. Natl. Acad. Sci. USA
88
2236-2240
1991
Bos taurus (Q07175), Bos taurus
brenda
Price, P.A.; Williamson, M.K.
Substrate recognition by the vitamin K-dependent gamma-glutamyl carboxylase: Identification of a sequence homology between the carboxylase and the carboxylase recognition site in the substrate
Protein Sci.
2
1987-1988
1993
Homo sapiens (P38435), Bos taurus (Q07175)
brenda
Wu, S.M.; Cheung, W.F.; Frazier, D.; Stafford, D.W.
Cloning and expression of the cDNA for human gamma-glutamyl carboxylase
Science
13
1634-1636
1991
Homo sapiens (P38435), Homo sapiens
brenda
Harbeck, M.C.; Cheung, A.Y.; Suttie, J.W.
Vitamin K-dependent carboxylase: partial purification of the enzyme by antibody affinity techniques
Thromb. Res.
56
317-323
1989
Bos taurus (Q07175), Bos taurus
brenda
Li, Q.; Schurgers, L.J.; Smith, A.C.; Tsokos, M.; Uitto, J.; Cowen, E.W.
Co-existent pseudoxanthoma elasticum and vitamin K-dependent coagulation factor deficiency: compound heterozygosity for mutations in the GGCX gene
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174
534-540
2009
Homo sapiens
brenda
Rai, A.J.; Udar, N.; Saad, R.; Fleisher, M.
A multiplex assay for detecting genetic variations in CYP2C9, VKORC1, and GGCX involved in warfarin metabolism
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55
823-826
2009
Homo sapiens
brenda
Qiao, J.; Wang, T.; Yang, J.; Liu, J.; Gong, X.; Guo, X.; Wang, S.; Ye, Z.
Genetic mutation of vitamin K-dependent gamma-glutamyl carboxylase domain in patients with calcium oxalate urolithiasis
J. Huazhong Univ. Sci. Technol. Med. Sci.
29
604-608
2009
Homo sapiens
brenda
Li, Q.; Uitto, J.
The mineralization phenotype in Abcc6 (-/-) mice is affected by Ggcx gene deficiency and genetic background--a model for pseudoxanthoma elasticum
J. Mol. Med.
88
173-181
2010
Mus musculus
brenda
Titapiwatanakun, R.; Rodriguez, V.; Middha, S.; Dukek, B.A.; Pruthi, R.K.
Novel splice site mutations in the gamma glutamyl carboxylase gene in a child with congenital combined deficiency of the vitamin K-dependent coagulation factors (VKCFD)
Pediatr. Blood Cancer
53
92-95
2009
Homo sapiens
brenda
Wang, T.; Yang, J.; Qiao, J.; Liu, J.; Guo, X.; Ye, Z.
Activity and expression of vitamin K-dependent gamma-glutamyl carboxylase in patients with calcium oxalate urolithiasis
Urol. Int.
85
94-99
2010
Homo sapiens
brenda
Krossy, C.; Lock, E.; rnsrud, R.
Vitamin K-dependent gamma-glutamylcarboxylase in Atlantic salmon (Salmo salar L.)
Fish Physiol. Biochem.
36
627-635
2010
Salmo salar
brenda
Rishavy, M.A.; Usubalieva, A.; Hallgren, K.W.; Berkner, K.L.
Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation
J. Biol. Chem.
286
7267-7278
2011
Homo sapiens
brenda
Wu, S.; Liu, S.; Davis, C.H.; Stafford, D.W.; Kulman, J.D.; Pedersen, L.G.
A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle
J. Theor. Biol.
279
143-149
2011
Homo sapiens (A7YA96)
brenda
King, C.R.; Deych, E.; Milligan, P.; Eby, C.; Lenzini, P.; Grice, G.; Porche-Sorbet, R.M.; Ridker, P.M.; Gage, B.F.
Gamma-glutamyl carboxylase and its influence on warfarin dose
Thromb. Haemost.
104
750-754
2010
Homo sapiens
brenda
Kaesler, N.; Schettgen, T.; Mutucumarana, V.P.; Brandenburg, V.; Jahnen-Dechent, W.; Schurgers, L.J.; Krueger, T.
A fluorescent method to determine vitamin K-dependent gamma-glutamyl carboxylase activity
Anal. Biochem.
421
411-416
2012
Rattus norvegicus
brenda
Haraikawa, M.; Tsugawa, N.; Sogabe, N.; Tanabe, R.; Kawamura, Y.; Okano, T.; Hosoi, T.; Goseki-Sone, M.
Effects of gamma-glutamyl carboxylase gene polymorphism (R325Q) on the association between dietary vitamin K intake and gamma-carboxylation of osteocalcin in young adults
Asia Pac. J. Clin. Nutr.
22
646-654
2013
Homo sapiens
brenda
Shiba, S.; Ikeda, K.; Azuma, K.; Hasegawa, T.; Amizuka, N.; Horie-Inoue, K.; Inoue, S.
gamma-Glutamyl carboxylase in osteoblasts regulates glucose metabolism in mice
Biochem. Biophys. Res. Commun.
453
350-355
2014
Mus musculus (Q3TME3)
brenda
Parker, C.H.; Morgan, C.R.; Rand, K.D.; Engen, J.R.; Jorgenson, J.W.; Stafford, D.W.
A conformational investigation of propeptide binding to the integral membrane protein gamma-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry
Biochemistry
53
1511-1520
2014
Homo sapiens
brenda
Vermeer, C.; van t Hoofd, C.; Knapen, M.H.J.; Xanthoulea, S.
Synthesis of 2-methyl-1,4-naphthoquinones with higher gamma-glutamyl carboxylase activity than MK-4 both in vitro and in vivo
Bioorg. Med. Chem. Lett.
27
208-211
2017
Homo sapiens, Rattus norvegicus
brenda
Nagahashi, K.; Umemura, K.; Kanayama, N.; Iwaki, T.
Successful synthesis of active human coagulation factor VII by co-expression of mammalian gamma-glutamyl carboxylase and modification of vit.K cycle in Drosophila Schneider S2 cells
Cytotechnology
69
317-327
2017
Mus musculus
brenda
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