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
-
6.4.1.1
-
phosphoenolpyruvate
-
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
- 6.4.1.1
- phosphoenolpyruvate
-
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
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Metals Ions
Metals Ions on EC 6.4.1.1 - pyruvate carboxylase
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Co2+
K+
KCl
Mg2+
Mn2+
NH4+
Zinc
Co2+
-
divalent cation required, activates with 58% of the efficiency relative to Mg2+
-
optimal concentration: 0.175 mM, activates at lower concentrations, inhibits at higher concentrations
Mg2+
-
the presence of MgCl2 in excess of ATP produces a more than 3fold activation
Mg2+
the biotin carboxylase domain requires divalent cations for binding of the ATP substrate and for catalysis
Mg2+
-
divalent metal required, Mg2+, and with lower efficiency Mn2+ or Co2+
Mg2+
essential 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. High Mg2+ concentration (above 7 mM) inhibits pyruvate carboxylation and MgATP cleavage but no inhibition of MgADP phosphorylation reaction
Mn2+
-
does not participate directly in the reaction mechanism, but may play a structural role essential to the integrity of the enzymes tetrameric structure
Mn2+
-
3fold activation in presence of MnCl2 equimolar in concentration to ATP
Mn2+
-
divalent metal ion required, Mg2+ or Mn2+. Mn2+ inhibits at concentrations above 1.25 mM
Mn2+
-
divalent cation required, activates with 66% of the efficiency relative to Mg2+
Mn2+
-
each subunit contains one tightly bound metal ion, predominantly Mn2+, or mixtures of Mn2+ and Mg2+
-
contains a tightly bound zinc atom per subunit of the tetramer. The metal has a role in catalysis but not apparently in the maintenance of the gross protein structure