4.1.1.90: peptidyl-glutamate 4-carboxylase
This is an abbreviated version!
For detailed information about peptidyl-glutamate 4-carboxylase, go to the full flat file.
Word Map on EC 4.1.1.90
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4.1.1.90
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calcification
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co2
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ribulose
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biotin
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acetyl-coa
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phosphoenolpyruvate
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arterial
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ribulose-1,5-bisphosphate
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chloroplast
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rubisco
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warfarin
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coagulation
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osteocalcin
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epoxide
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bisphosphate
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1,5-bisphosphate
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propionyl
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spinach
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gamma-carboxylation
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osteopontin
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biotin-dependent
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gamma-carboxyglutamic
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4.1.1.39
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prothrombin
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propeptide
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rubp
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calcify
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osteoprotegerin
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acidemia
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rhodospirillum
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biotinidase
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propionyl-coa
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rubrum
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rbcl
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pepcs
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vkorc1
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fetuin-a
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accase
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photorespiration
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osteonectin
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phylloquinone
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crassulacean
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pseudoxanthoma
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undercarboxylated
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elasticum
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medicine
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co2-fixing
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carboxysomes
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flaveria
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synthesis
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carboxy-lyase
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phosphoribulokinase
- 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
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pepcs
- vkorc1
- fetuin-a
- accase
-
photorespiration
- osteonectin
- phylloquinone
-
crassulacean
-
pseudoxanthoma
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undercarboxylated
- elasticum
- medicine
-
co2-fixing
- carboxysomes
- flaveria
- synthesis
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carboxy-lyase
- phosphoribulokinase
Reaction
Synonyms
carboxylase, Ci-GGC, gamma glutamyl carboxylase, gamma-carboxylase, gamma-glutamyl carboxylase, GGCX, glutamate carboxylase, matrix gamma-carboxyglutamate protein, matrix Gla protein, peptidyl-glutamate 4-carboxylase, peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing), two-chain carboxylase, vitamin K carboxylase, vitamin K-dependent carboxylase, vitamin K-dependent gamma-glutamyl carboxylase, vitamin K-dependent gamma-glutamylcarboxylase, VKC, VKD carboxylase
ECTree
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Engineering
Engineering on EC 4.1.1.90 - peptidyl-glutamate 4-carboxylase
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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
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transmembrane domain residues in the C-terminal peptide to test for polar/charge residues
G363L/T367L
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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
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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
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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
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
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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
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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
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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
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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
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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
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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