6.4.1.1: pyruvate carboxylase
This is an abbreviated version!
For detailed information about pyruvate carboxylase, go to the full flat file.
Word Map on EC 6.4.1.1
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6.4.1.1
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phosphoenolpyruvate
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gluconeogenesis
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carboxykinase
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biotin
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oxaloacetate
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acetyl-coa
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tricarboxylic
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gluconeogenic
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anaplerotic
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malate
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citrate
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tca
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co2
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malic
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pepck
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carboxylases
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astrocyte
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glucose-6-phosphatase
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biotin-dependent
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acidosis
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propionyl-coa
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citric
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krebs
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glutamicum
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bark
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pine
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biotin-containing
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13c-labeled
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propionyl
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isotopomer
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maritime
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1-13cglucose
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avidin
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hyperammonemia
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fructose-1,6-diphosphatase
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carboxyltransferase
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pyrogenic
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4.1.1.32
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1,6-bisphosphatase
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holocarboxylase
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transcarboxylase
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biotinidase
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pyrolytic
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leigh
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ureagenesis
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medicine
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glucogenic
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biotechnology
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penicillinase
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13c-enriched
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pinaster
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synthesis
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3-methylcrotonyl-coa
- 6.4.1.1
- phosphoenolpyruvate
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gluconeogenesis
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carboxykinase
- biotin
- oxaloacetate
- acetyl-coa
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tricarboxylic
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gluconeogenic
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anaplerotic
- malate
- citrate
- tca
- co2
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malic
- pepck
- carboxylases
- astrocyte
- glucose-6-phosphatase
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biotin-dependent
- acidosis
- propionyl-coa
-
citric
-
krebs
- glutamicum
-
bark
- pine
-
biotin-containing
-
13c-labeled
-
propionyl
-
isotopomer
-
maritime
-
1-13cglucose
- avidin
- hyperammonemia
-
fructose-1,6-diphosphatase
- carboxyltransferase
-
pyrogenic
-
4.1.1.32
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1,6-bisphosphatase
- holocarboxylase
- transcarboxylase
- biotinidase
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pyrolytic
- leigh
-
ureagenesis
- medicine
-
glucogenic
- biotechnology
- penicillinase
-
13c-enriched
- pinaster
- synthesis
- 3-methylcrotonyl-coa
Reaction
Synonyms
Carboxylase, pyruvate, EhPYC1, HpPyc1p, Mfla_1512, MSmeg_2412, PC, Pcase, PCB, PCC, PCx, PYC, Pyc1, Pyc1p, PYC2, pycA, pyruvate carboxylase, pyruvate carboxylase 1, Pyruvic carboxylase, RePC
ECTree
6.4.1.1 pyruvate carboxylaseAdvanced search results
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results (Engineering
Engineering on EC 6.4.1.1 - pyruvate carboxylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K1112A
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site-directed mutagenesis, the mutant lacks the biotin binding site and boud biotin, it does not catalyse the complete reaction, but catalyses ATP-cleavage and the carboxylation of free biotin. Oxaloacetate decarboxylation is not catalysed, even in the presence of free biotin, suggesting that only the biotin carboxylation domain of the enzyme is accessible to free biotin. The mutant K1112A also catalyses the phosphorylation of ADP from carbamoyl phosphate
A610T
M743I
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A
R451C
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant enzyme shows markedly decreased acetyl-CoA-dependent activation
V145A
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A
G746A
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mutation to corresponding Entercoccus faecalis residue. Mutant shows similar activity as wild-type, mutation reduces inhibition by cyclic di-3',5'-adenosine monophosphate to 40%, compared to 60% for wild-type
Y715T
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mutation to correspoinding human residue. Mutant shows similar activity as wild-type, mutation abolishes inhibition by cyclic di-3',5'-adenosine monophosphate
A465R
mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
D502A/E507A
mutation in the alpha subunit, mutant forms a stable holoenzyme, about 40% of wild-type activity
H476A/E478A
mutation in the alpha subunit, mutant forms a stable holoenzyme and is fully active
H476A/E478A/D502A/E507A
mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
K419A/E421A/E422A
mutations bin the beta subunit designed to reduce the surface entropy. The mutations have no effect on the catalytic activity of the enzyme
Q452stop
mutation in the alpha subunit, abolishes the formation of the holoenzyme
R401E
mutation in the alpha subunit, mutant forms a stable holoenzyme, about 50% of wild-type activity
A465R
Methylobacillus flagellatus DSM 6875
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mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
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H476A/E478A
Methylobacillus flagellatus DSM 6875
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mutation in the alpha subunit, mutant forms a stable holoenzyme and is fully active
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K419A/E421A/E422A
Methylobacillus flagellatus DSM 6875
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mutations bin the beta subunit designed to reduce the surface entropy. The mutations have no effect on the catalytic activity of the enzyme
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Q452stop
Methylobacillus flagellatus DSM 6875
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mutation in the alpha subunit, abolishes the formation of the holoenzyme
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R401E
Methylobacillus flagellatus DSM 6875
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mutation in the alpha subunit, mutant forms a stable holoenzyme, about 50% of wild-type activity
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Y542V/A557Q/S762D
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the triple mutation fully inactivates the moonlighting function of Pyc1, but not the enzyme activity of pyruvate carboxylase
A55T
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mutation in the beta subunit, reduces activity by 50fold and interferes with biotin binding to the active site,mutant exhibits growth on pyruvate similar to the wild type
K572A
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mutation in the beta subunit, abolishes biotinylation and leads to growth defects in pyruvate that are similar to that of a gene deletion mutant
D1018A
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
D420A
mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA
E1027A
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
E1027R
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
H216N
no differences to quarterny structures compared to wild-type. Mutation results in a 9fold increase in the Km for MgATP in its steady-state cleavage in the absence of pyruvate and a 3fold increase in the Km for MgADP in its steady-state phosphorylation by carbamoyl phosphate. kcat/Km (MgATP)98% decreased compared to wild-type. For MgADP phosphorylation kcat/Km is 99.5% decreased compared to wild-type. The Kd of the enzyme MgATP complex is essentially the same in the wildtype enzyme and H216N but the first-order rate constant for MgATP cleavage in the single-turnover experiments in H216N is only 0.75% of that for the wild-type enzyme, and thus, the MgATP cleavage step is rate-limiting in the steady state for H216N but not for the wild-type enzyme
K1119Q
mutant that lacks tethered biotin. Addition of 10 mM biotin increases the kcat of MgATP hydrolysis to rates observed for wild-type RePC in the absence of free biotin. This rate increase, coupled with a 35fold decrease in the Km for MgATP, results in a nearly 1000fold increase in the catalytic efficiency of the mutant K1119Q RePC catalyzed reaction when 10 mM free biotin is added
K119Q
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no catalytic acitivy for pyruvate decarboxylation, or oxaloacetate decarboxylation
K718Q
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2.9% of wild-type activity for pyruvate carboxylation, 14% for full reverse reaction, 7.2% for oxaloacetate decarboxylation in presence of oxamate
Q552A
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
Q552N
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
Q844L/S885A
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13% of wild-type activity for pyruvate carboxylation, 53% for full reverse reaction, 4.7% for oxaloacetate decarboxylation in presence of oxamate
R424
mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA. Mutation decreases the activation enthalpy of the pyruvate carboxylation reaction by an amount consistent with removal of a single hydrogen bond
R427K
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 76fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 2.6fold higher compared to wild-type, kcat/Km value 12% of wild-type. Ka (activation value) for Mg2+ is 8fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.4% of wild-type in the presence of acetyl-CoA/0.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 21% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type. residual activity at saturating concentrations of L-aspartate is 2fold greater than wild-type
R427S
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 15fold higher compared to wild-type, kcat 41% of wild-type enzyme, Km (MgATP) 1.5fold higher compared to wild-type, kcat/Km value 26% of wild-type. Ka (activation value) for Mg2+ is 2fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 1.1% of wild-type in the presence of acetyl-CoA/5.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 17% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity similar to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type
R429S
residue Arg429 is especially important for acetyl CoA binding. Mutation results in a 100fold increase in the Ka of acetyl-CoA activation and a large decrease in the cooperativity of this activation
R469K
mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
R469S
mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
R472K
45% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 252fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 6.7fold higher compared to wild-type, kcat/Km value 3% of wild-type. Ka (activation value) for Mg2+ is 37fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-tpye in the presence of acetyl-CoA/0.9% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 8% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 3% biotin carboxylation rate of wild-type
R472S
R548A
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
R548K
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the mutation results in loss of the ability to catalyse pyruvate carboxylation (2% residual activity), biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
T882A
T882C
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7.1% of wild-type activity for pyruvate carboxylation, 20% for full reverse reaction, 11% for oxaloacetate decarboxylation in presence of oxamate
T882S
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21% of wild-type activity for pyruvate carboxylation, 51% for full reverse reaction, 30% for oxaloacetate decarboxylation in presence of oxamate
D420A
Rhizobium etli ATCC 51251
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mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA
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E1027A
Rhizobium etli ATCC 51251
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mutant has increased activity in the absence of acetyl-CoA, but not in its presence
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E1027R
Rhizobium etli ATCC 51251
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mutant has increased activity in the absence of acetyl-CoA, but not in its presence
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R424
Rhizobium etli ATCC 51251
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mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA. Mutation decreases the activation enthalpy of the pyruvate carboxylation reaction by an amount consistent with removal of a single hydrogen bond
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R429K
Rhizobium etli ATCC 51251
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enhances the activity of the enzyme in the absence of acetyl-CoA
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R429S
Rhizobium etli ATCC 51251
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residue Arg429 is especially important for acetyl CoA binding. Mutation results in a 100fold increase in the Ka of acetyl-CoA activation and a large decrease in the cooperativity of this activation
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R469K
Rhizobium etli ATCC 51251
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mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
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R469S
Rhizobium etli ATCC 51251
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mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
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H216N
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no differences to quarterny structures compared to wild-type. Mutation results in a 9fold increase in the Km for MgATP in its steady-state cleavage in the absence of pyruvate and a 3fold increase in the Km for MgADP in its steady-state phosphorylation by carbamoyl phosphate. kcat/Km (MgATP)98% decreased compared to wild-type. For MgADP phosphorylation kcat/Km is 99.5% decreased compared to wild-type. The Kd of the enzyme MgATP complex is essentially the same in the wildtype enzyme and H216N but the first-order rate constant for MgATP cleavage in the single-turnover experiments in H216N is only 0.75% of that for the wild-type enzyme, and thus, the MgATP cleavage step is rate-limiting in the steady state for H216N but not for the wild-type enzyme
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K1119Q
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mutant that lacks tethered biotin. Addition of 10 mM biotin increases the kcat of MgATP hydrolysis to rates observed for wild-type RePC in the absence of free biotin. This rate increase, coupled with a 35fold decrease in the Km for MgATP, results in a nearly 1000fold increase in the catalytic efficiency of the mutant K1119Q RePC catalyzed reaction when 10 mM free biotin is added
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R427K
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more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 76fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 2.6fold higher compared to wild-type, kcat/Km value 12% of wild-type. Ka (activation value) for Mg2+ is 8fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.4% of wild-type in the presence of acetyl-CoA/0.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 21% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type. residual activity at saturating concentrations of L-aspartate is 2fold greater than wild-type
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R427S
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more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 15fold higher compared to wild-type, kcat 41% of wild-type enzyme, Km (MgATP) 1.5fold higher compared to wild-type, kcat/Km value 26% of wild-type. Ka (activation value) for Mg2+ is 2fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 1.1% of wild-type in the presence of acetyl-CoA/5.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 17% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity similar to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type
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R472K
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45% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 252fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 6.7fold higher compared to wild-type, kcat/Km value 3% of wild-type. Ka (activation value) for Mg2+ is 37fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-tpye in the presence of acetyl-CoA/0.9% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 8% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 3% biotin carboxylation rate of wild-type
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R472S
-
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 203fold higher compared to wild-type, kcat 25% of wild-type enzyme, Km (MgATP) 8.7fold higher compared to wild-type, kcat/Km value 2% of wild-type. Ka (activation value) for Mg2+ is 30fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-type in the presence of acetyl-CoA/1.2% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 5% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 2% biotin carboxylation rate of wild-type
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T882A
-
T882 mutant is a tetrameric holoenzyme where positioning of the tethered biotin favors placement in the BC domain. Free biotin increases the kcat for both the wild-type and the T882A mutant RePC-catalyzed reactions without having a major effect on the Km for MgATP. Crystal structures of mutant T882A pyruvate carboxylase are determined cocrystallized with phosphonoacetate and MgADP
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E40R
predominant form of mutant E40R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
E433R
predominant form of mutant E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
R36E
the R36E is much more susceptible to tetramer dissociation and inactivation than the wild type enzyme. Coexpression of mutant forms with wild type Pyc1 shows that the R36E mutation had no effect on the interaction of these subunits with those of wild type Pyc1
R36E/E433R
predominant form of mutant R36E/E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
additional information
A610T
-
naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant's catalytic activity and steady-state level are markedly decreased
R472S
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the mutation severely decreases the affinity of the enzyme for acetyl-CoA
R472S
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 203fold higher compared to wild-type, kcat 25% of wild-type enzyme, Km (MgATP) 8.7fold higher compared to wild-type, kcat/Km value 2% of wild-type. Ka (activation value) for Mg2+ is 30fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-type in the presence of acetyl-CoA/1.2% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 5% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 2% biotin carboxylation rate of wild-type
T882A
-
no catalytic activity for reactions involving the carboxyl transferase domain. 7- and 3.5fold increases in activity, as compared to that of the wild-type enzyme, for the ADP phosphorylation and bicarbonate-dependent ATPase reactions, respectively. Partial inhibition of the T882A-catalyzed biotin carboxylase domain reactions by oxamate and pyruvate
T882A
T882 mutant is a tetrameric holoenzyme where positioning of the tethered biotin favors placement in the BC domain. Free biotin increases the kcat for both the wild-type and the T882A mutant RePC-catalyzed reactions without having a major effect on the Km for MgATP. Crystal structures of mutant T882A pyruvate carboxylase are determined cocrystallized with phosphonoacetate and MgADP
additional information
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a chimeric enzyme mutant, comprising the biotin carboxylase domain of the enzyme from Aquifex aeolicus and the transcarboxylation and BCCP domain from Bacillus thermodenitrificans, shows an activity that is independent of acetyl-CoA, a characteristic of the Aquifex aeolicus enzyme and not the Bacillus thermodentrificans enzyme
additional information
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polypeptide chain is divided into two chains, between the biotin carboxylase and carboxyltransferase domains, resulting in two proteins PC-(BC) and PC-(CT+BCCP) with retained enzyme activity
additional information
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construction of an enzyme mutant form, in which the lysine residue to which the biotin is normally covalently bound is mutated to an alanine residue, this results in the production of an unbiotinylated apo-enzyme, which can, however, carboxylate free biotin in a reaction that proceeds 8fold faster in the presence of acetyl-CoA than in its absence. A chimeric enzyme mutant, comprising the biotin carboxylase domain of the nezyme from Aquifex aeolicus and the transcarboxylation and BCCP domain from Bacillus thermodenitrificans, shows an activity that is independent of acetyl-CoA, a characteristic of the Aquifex aeolicus enzyme and not the Bacillus thermodentrificans enzyme
additional information
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molecular basis of pyruvate carboxylase deficiency, mosaicism correlates with prolonged survival, three clinical phenotypes: type A is an infantile form, type B is a neonatal form, and type Casa benign form. Analysis of combinations of missense mutations, deletions, a splice site substitution and a nonsense mutation, overview
additional information
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three forms of PC deficiency are classified. Type A or the North American phenotype is caused by several point mutations and characterized by a mild lactic acidaemia but a normal ratio of plasma lactate to pyruvate, psychomotor retardation and in some, but not all cases, death in the first years of life. type B phenotype, a complex genotype in which two deletion mutations in both PC alleles was identified, i.e. one allele possesses two nucleotide deletions in exon 16, creating a frameshift mutation, whereas the other allele possesses four nucleotide deletions in intron 15, resulting in an aberrant transcript. These two mutations generate premature terminations of the protein. The type C or benign phenotype is characterized as a mild lactic acidosis but normal psychomotor development
additional information
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transgenic mice carrying a dominant-negative mutant CREB show a global reduction of gluconeogenic enzymes including PC, PEPCK and glucose 6-phosphatase
additional information
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deletion of the PC gene in this yeast impairs alcohol oxidase activity, causing the accumulation of inactive alcohol oxidase in the cytosol
additional information
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mutant strain STM5437contains an insertion in the PA5437 or pycR gene encoding for a pyruvate carboxylase regulator, PycR inactivation results in 100000fold attenuation of virulence in the rat lung in vivo, phenotype, overview
additional information
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overexpression of v-MAFA in INS1 cells causes a 5fold increase of pyruvate carboxylase mRNA
additional information
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stable overexpression of the enzyme in INS-1 cells leads to significantly upregulated insulin secretion and cell proliferation, while enzyme downregulation by siRNA expression reduces insulin secretion and cell proliferation, phenotypes, overview
additional information
suppression by stable expression of siRNA causes impaired anaplerosis and insulin secretion in insulinoma cells, knockout in INS-1 832/13 cells, cell lines U6 and CHS, and in INS-1 832/13-derived cell lines PCX3, PC1971, PC1973, PC3064, and PC118. Insulin release in response to pyruvate alone, 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid plus glutamine, or methyl succinate plus beta-hydroxybutyrate is also decreased in the PC knockdown cells, phenotype, overview
additional information
construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
additional information
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construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
additional information
generation of functional, mixed hybrid tetramers using the E218A (inactive biotin carboxylase domain) and T882S (low pyruvate binding, low activity) mutant forms of pyruvate carboxylase. The apparent Ka pyruvate for the pyruvate-stimulated release of Pi by the hybrid tetramer is comparable to the wild-type enzyme and nearly 10fold lower than that for the T882S homotetramer. The ratio of the rates of oxaloacetate formation to Pi release for the WT:T882S[1:1] complex and 218A:T882S[1:1] hybrid tetramer-catalyzed reactions is 0.5 and 0.6, respectively, while the T882S homotetramer exhibits a near 1:1 coupling of the two domains
additional information
Rhizobium etli ATCC 51251
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construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
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additional information
Rhizobium etli ATCC 51251
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generation of functional, mixed hybrid tetramers using the E218A (inactive biotin carboxylase domain) and T882S (low pyruvate binding, low activity) mutant forms of pyruvate carboxylase. The apparent Ka pyruvate for the pyruvate-stimulated release of Pi by the hybrid tetramer is comparable to the wild-type enzyme and nearly 10fold lower than that for the T882S homotetramer. The ratio of the rates of oxaloacetate formation to Pi release for the WT:T882S[1:1] complex and 218A:T882S[1:1] hybrid tetramer-catalyzed reactions is 0.5 and 0.6, respectively, while the T882S homotetramer exhibits a near 1:1 coupling of the two domains
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additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
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construction of chimeric enzymes of Pyc1 and Pyc2
additional information
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50% down-regulation of the enzyme in the RTG1 and the RTG2 mutants
additional information
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construction of chimeric enzymes of Pyc1 and Pyc2
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