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
-
carboxykinase
- biotin
- oxaloacetate
- acetyl-coa
-
tricarboxylic
-
gluconeogenic
-
anaplerotic
- malate
- citrate
- tca
- co2
-
malic
- pepck
- carboxylases
- astrocyte
- glucose-6-phosphatase
-
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
-
1,6-bisphosphatase
- holocarboxylase
- transcarboxylase
- biotinidase
-
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
results (
results (Activating Compound
Activating Compound on EC 6.4.1.1 - pyruvate carboxylase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate
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allosteric activator of pyruvate carboxylase. The increase in activity between 2 mM and saturating MgATP is approximately 16fold
acetoacetyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
malonyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
n-butanoyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
n-propanoyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
oleoyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
oxamate
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oxamate acts as a carboxyl acceptor, forming a carbamylated oxamate product and thereby accelerating the enzymatic decarboxylation reaction
TNFalpha
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pyruvate decarboxylase activity decreases in TNFalpha-sensitive cells but increases in bcl-2 transfected cells
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acetyl CoA
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enzyme activator, major effect is to promote the carboxylation of biotin, reduces the Kms for both MgATP2- and biotin, overview
acetyl-CoA
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in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 4% of that obtained in presence of saturating concentrations of acetyl-CoA
acetyl-CoA
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activates in presence of either L-Asp or 2-oxoglutarate but does not activate in absence of these dicarboxylic acids. Trinitrobenzenesulfonate causes selective loss of the capacity for activation by acetyl-CoA
acetyl-CoA
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in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 20% of that obtained in presence of saturating concentrations of acetyl-CoA
acetyl-CoA
allosteric activator, 50% of maximal activity at 0.013 mM for the recombinant enzyme and at 0.015 mM for the liver enzyme
acetyl-CoA
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in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 21% of that observed in the presence of saturating concentrations of the activator
acetyl-CoA
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allosteric activator of pyruvate carboxylase, there is a 7fold increase in the turnover number for ATP cleavage induced by acetyl-CoA
acetyl-CoA
nonessential activator. Both acetyl-CoA and Mg2+ assist in coupling the MgATP-dependent carboxylation of biotin in the biotin carboxylase (BC) domain with pyruvate carboxylation in the carboxyl transferase (CT) domain. Absence of acetyl-CoA results in only 9% of fully activated enzyme. Acetyl-CoA also has a noticeable effect on the activity of the oxamate-induced decarboxylation of oxaloacetate but no effect on the rate of MgADP phosphorylation by carbamoyl phosphate
acetyl-CoA
acetyl-CoA acts to decrease the activation free energy of the reaction by both increasing the activation entropy and decreasing the activation enthalpy
acetyl-CoA
the substrates of the biotin carboxylase and carboxyl transferase domain are energetically coupled in the presence of acetyl-CoA. Both kinetic and energetic coupling between the two domains is lost in the absence of acetyl-CoA
acetyl-CoA
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activation in decreasing order: acetyl-CoA, n-propanoyl-CoA, n-butanoyl-CoA, malonyl-CoA, CoA, acetoacetyl-CoA, oleoyl-CoA
acetyl-CoA
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allosteric activator. Concentrations eliciting maximal activity are 0.013 mM, 0.042 mM and 0.084 mM at assay temperatures of 45°C, 55°C, and 65°C respectively
acyl-CoA derivatives
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activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
additional information
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starvation enhances pyruvate carboxylase activity. Short-term treatment with glucagon increases pyruvate carboxylase mRNA but does not result in an apparent change in protein levels or activity. Pyruvate carboxylase and PEP carboxykinase acts cooperatively
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additional information
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starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
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additional information
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starvation enhances pyruvate carboxylase activity. Peroxisome-proliferator-activated receptor gamma increases enzyme expression in adipocytes. Rosiglitazone or other thiazolidinediones induce the enzyme expression. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
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additional information
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activity strongly influenced by the carbon source used for growth
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additional information
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starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
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additional information
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acetyl-CoA and K+ have no effect on ADP phosphorylation by carbamoyl phosphate
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