4.1.1.32: phosphoenolpyruvate carboxykinase (GTP)
This is an abbreviated version!
For detailed information about phosphoenolpyruvate carboxykinase (GTP), go to the full flat file.
Word Map on EC 4.1.1.32
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4.1.1.32
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biliary
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cirrhosis
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gluconeogenesis
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autoantigens
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autoimmune
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gluconeogenic
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autoantibody
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epitope
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lipoylated
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antimitochondrial
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camp
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glucocorticoid
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bile
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immunodominant
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malate
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malic
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autoreactive
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cholangitis
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intrahepatic
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lipoic
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autoepitope
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glyceroneogenesis
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dibutyryl
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6.4.1.1
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anaplerotic
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3-mercaptopicolinic
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2.7.1.40
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bt2camp
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pbc-specific
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fto-2b
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oxalacetate
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2-oxo-acid
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ama-positive
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dihydrolipoamide
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self-tolerance
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drug development
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synthesis
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pharmacology
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medicine
- 4.1.1.32
- biliary
- cirrhosis
-
gluconeogenesis
- autoantigens
- autoimmune
-
gluconeogenic
- autoantibody
- epitope
-
lipoylated
-
antimitochondrial
- camp
- glucocorticoid
- bile
-
immunodominant
- malate
-
malic
-
autoreactive
- cholangitis
-
intrahepatic
-
lipoic
-
autoepitope
-
glyceroneogenesis
-
dibutyryl
-
6.4.1.1
-
anaplerotic
-
3-mercaptopicolinic
-
2.7.1.40
-
bt2camp
-
pbc-specific
-
fto-2b
- oxalacetate
- 2-oxo-acid
-
ama-positive
- dihydrolipoamide
-
self-tolerance
- drug development
- synthesis
- pharmacology
- medicine
Reaction
Synonyms
C4 phosphoenolpyruvate carboxykinase, carboxykinase, phosphopyruvate (guanosine triphosphate), CGI_10014916, CgPCK, GDP-linked PEP carboxykinase, GTP-dependent PEPCK-C, GTP-PEPCK, GTP/ITP: oxaloacetate carboxylase (transphosphorylating), GTP/ITP:oxaloacetate carboxylyase (transphosphorylating), GTP/ITP:oxaloacetatecarboxylase (transphosphorylating), GTP:oxaloacetate carboxy-lyase, oxaloacetate kinase (decarboxylating, GDP), P-enolpyruvate carboxykinase, PCK, PCK2, PDC-E2, PEP carboxykinase, PEP carboxylase, PEP-carboxykinase, PEPC, PEPCK, PEPCK-C, PEPCK-M, phosphoenolpyruvate carboxykinase, phosphoenolpyruvate carboxykinase (GTP), phosphoenolpyruvate carboxykinase, GTP-dependent, Phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxylase (GTP), phosphoenolpyruvic carboxykinase, phosphoenolpyruvic carboxykinase (GTP), phosphoenolpyruvic carboxykinase (inosine triphosphate), Phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxylase (GTP), phosphoenolpyruvic carboxylase (inosine triphosphate), phosphopyruvate carboxykinase, phosphopyruvate carboxylase, phosphopyruvate carboxylase (GTP)
ECTree
4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)Advanced search results
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results (Metals Ions
Metals Ions on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP)
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Co2+
Fe2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Co2+
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divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Co2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Co2+: 0.752 mM. When Mg2+ is added as a second cation, in presemce of Mg2+, the Km values for CO2+ in both directions of the reaction are markedly decreased
Fe2+
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Fe2+ alone does not stimulate, Fe2+ + ferroactivator, stimulate in both directions of the reaction
Fe2+
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0.05 mM FeCl2 and 0.0044 mg/ml ferroactivator, enhance to 3.1times the unstimulated rate. 1.5 mM FeCl2 causes rapid inactivation
Mg2+
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absolute requirement of a metal ion, activity is maximal in the presence of both Mn2+ and Mg2+, for single ion activation Mn2+ can be substituted by Mg2+ with a reduced enzyme activity
Mg2+
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mg2+
requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+
Mg2+
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divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mg2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Mg2+: 5.36 mM. When Mg2+ is added as a second cation, the Km values for Mn2+ in both directions of the reaction are markedly decreased to 0.021-0.022 mM
Mn2+
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enzyme-bound, role of His-225 and Asp-263 in Mn2+ binding, Asp-262 and Thr-249 are also part of the metal binding sites
Mn2+
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binds directly to the enzyme and binds to the nucleotide resulting in the metal-nucleotide complex
Mn2+
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enzyme binds Mn2+ at the catalytic site, binary PEPCK-Mn2+ complex, activator Mn2+ enhances the nucleotide binding
Mn2+
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absolute requirement of a metal ion, activity is maximal in the presence of both Mn2+ and Mg2+, for single ion activation Mn2+ can be substituted by Mg2+ with a reduced enzyme activity
Mn2+
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mn2+
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best activator, enzyme requires two divalent cations, one activates through a direct interaction with enzyme at site n1, located at Asp-295 and Asp-296, the second cation, at site n2, acts in the cation-nucleotide complex that serves as a substrate, role and binding mode of Mn2+, may be a regulator for enzyme in vivo
Mn2+
the IC50 values for Mn2+ are 0.009 mM for Mg2+ concentration 2 mM, wild-type, Vmax = 31 micromol/min/mg, 0.607 mM for Mg2+ concentration 2 mM, Y235F mutant, Vmax = 4 micromol/min/mg, 0.073 mM for Mg2+ concentration 2 mM, Y235A mutant, Vmax = 19 micromol/min/mg, 0.058 mM for Mg2+ concentration 2 mM, Y235S mutant, Vmax = 13 micromol/min/mg, 0.0008 mM for wild-type, Vmax = 29 micromol/min/mg, 0.0007 mM for Y235F mutant, Vmax = 31 micromol/min/mg, 0.0004 mM for Y235A mutant, Vmax = 2 micromol/min/mg, 0.0007 mM for Y235S mutant, Vmax = 2 micromol/min/mg, 0.009 mM for wild-type, Mg2+ concentration 5 mM, Vmax = 31 micromol/min/mg, 0.562 mM for Y235F mutant, Mg2+ concentration 5 mM, Vmax = 4 micromol/min/mg, 0.064 mM for Y235A mutant, Mg2+ concentration 5 mM, Vmax = 18 micromol/min/mg, 0.048 mM for Y235S mutant, Mg2+ concentration 5 mM, Vmax = 13 micromol/min/mg, 0.009 mM for wild-type, Mg2+ concentration 7.5 mM, Vmax = 31 micromol/min/mg, 0.521 mM for Y235F mutant, Mg2+ concentration 7.5 mM, Vmax = 4 micromol/min/mg, 0.057 mM for Y235A mutant, Mg2+ concentration 7.5 mM, Vmax = 18 micromol/min/mg, 0.043 mM for Y235S mutant, Mg2+ concentration 7.5 mM, Vmax = 13 micromol/min/mg
Mn2+
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half-maximal activation: of phosphoenolpyruvate carboxylation at 2 mM, of oxaloacetate decarboxylation at 0.4 mM, of exchange reaction at 8 mM
Mn2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Mn2+
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divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mn2+
divalent cation required for reaction, highest activity with Mn2+
Mn2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Km for Mn2+: 0.263 mM. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+
Zn2+
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divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
additional information
not activated by Ca2+, Zn2+, Cu2+ or Ni2+
additional information
no activity with Ca2+, Zn2+, Cu2+, Ni2+, and Sr2+
