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Information on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP) and Organism(s) Thermococcus kodakarensis and UniProt Accession Q6F494
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4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)IUBMB Comments
ITP can act as phosphate donor.
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Word Map
- 4.1.1.32
- biliary
- cirrhosis
-
gluconeogenesis
- autoantigens
- autoimmune
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gluconeogenic
- autoantibody
- epitope
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lipoylated
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antimitochondrial
- camp
- glucocorticoid
- bile
-
immunodominant
- malate
-
malic
-
autoreactive
- cholangitis
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intrahepatic
-
lipoic
-
autoepitope
-
glyceroneogenesis
-
dibutyryl
-
6.4.1.1
-
anaplerotic
-
3-mercaptopicolinic
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2.7.1.40
-
bt2camp
-
pbc-specific
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fto-2b
- oxalacetate
- 2-oxo-acid
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ama-positive
- dihydrolipoamide
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self-tolerance
- drug development
- synthesis
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pdc-e2, pepck-c, pep carboxykinase, p-enolpyruvate carboxykinase, phosphoenolpyruvate carboxykinase (gtp), pepck-m, pep-carboxykinase, phosphopyruvate carboxylase, phosphopyruvate carboxykinase, gtp:oxaloacetate carboxy-lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxykinase, phosphopyruvate (guanosine triphosphate)
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oxaloacetate kinase (decarboxylating, GDP)
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P-enolpyruvate carboxykinase
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PEP carboxykinase
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PEP carboxylase
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PEPCK
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phosphoenolpyruvate carboxykinase
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Phosphoenolpyruvate carboxylase
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phosphoenolpyruvate carboxylase (GTP)
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phosphoenolpyruvic carboxykinase
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phosphoenolpyruvic carboxykinase (GTP)
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phosphoenolpyruvic carboxykinase (inosine triphosphate)
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Phosphoenolpyruvic carboxylase
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phosphoenolpyruvic carboxylase (GTP)
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phosphoenolpyruvic carboxylase (inosine triphosphate)
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-
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phosphopyruvate carboxykinase
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phosphopyruvate carboxylase
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phosphopyruvate carboxylase (GTP)
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
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-
-
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decarboxylation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
GTP:oxaloacetate carboxy-lyase (adding GTP; phosphoenolpyruvate-forming)
ITP can act as phosphate donor.
CAS REGISTRY NUMBER
COMMENTARY
9013-08-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
poor substrate
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
poor activity
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-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
first committed step of gluconeogenesis, important enzyme in the interconversion between C3 and C4 metabolites, recycling of an excess of phosphoenolpyruvate produced from pyruvate
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-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon
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-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
the enzyme prefers phosphoenolpyruvate formation from oxaloacetate
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-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
ITP and IDP act as alternative nucleotide cofactors with similar Vmax values and slightly higher Km values
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-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
first committed step of gluconeogenesis, important enzyme in the interconversion between C3 and C4 metabolites, recycling of an excess of phosphoenolpyruvate produced from pyruvate
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon
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-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
additional information
no activity with Ca2+, Zn2+, Cu2+, Ni2+, and Sr2+
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
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+
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
pH 6.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 90
50°C: about 45% of maximal activity, 90°C: about 80% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hyperthermophilic archaeon, highest enzyme level when grown with pyruvate as substrate
SwissProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72036
4 * 72036, subunit mass calculated from the deduced amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
4 * 72036, subunit mass calculated from the deduced amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Release 2023.1 (January 2023)
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