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Information on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP) and Organism(s) Mycolicibacterium smegmatis and UniProt Accession Q9AGJ6

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)
IUBMB Comments
ITP can act as phosphate donor.
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This record set is specific for:
Mycolicibacterium smegmatis
UNIPROT: Q9AGJ6
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Word Map
The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GTP/ITP:oxaloacetate carboxylyase (transphosphorylating)
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phosphoenolpyruvate carboxykinase, GTP-dependent
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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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-
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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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phosphopyruvate carboxykinase
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-
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phosphopyruvate carboxylase
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phosphopyruvate carboxylase (GTP)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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-
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decarboxylation
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-
-
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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 hide
9013-08-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
r
additional information
?
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ADP is a very poor substrate in the reverse reaction
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Mg2+
requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+
Mn2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
additional information
not activated by Ca2+, Zn2+, Cu2+ or Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-ketoglutarate
inhibits oxaloacetate formation, mixed-type inhibition
KCl
0.5 M, 50% inhibition
NaCl
0.5 M, 50% inhibition
oxalate
potent inhibitor of oxaloacetate formation, mixed-type inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
maximum stimulation at 75 mM
dithiothreitol
maximum at 10-40 mM, 30% stimulation
reduced glutathione
maximum stimulation at 20 mM
thiol-containing reducing agent
activates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.3
CO2
pH 7.2, 37°C, bicarbonate
0.066
GDP
pH 7.2, 37°C
0.013
GTP
pH 7.2, 37°C
0.29
IDP
pH 7.2, 37°C
0.0067 - 0.0189
oxaloacetate
0.1
phosphoenolpyruvate
pH 7.2, 37°C
additional information
additional information
Km-values for several divalent cations, the presence of 2 mM Mg2+ greatly lowers the Km-values for Mn2+, 144fold in the presence of dithiothreitol and 9.4fold in the absence of dithiothreitol, and for Co2+ by 230fold, influence of divalent cations on the Km-value for phosphoenolpyruvate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
mutant enzyme D78A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
0.13
mutant enzyme D78A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
0.15
mutant enzyme D78A, oxaloacetate-forming activity in the presence of 2 mM Mn2+
0.36
mutant enzyme E83A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
0.4
mutant enzyme E83A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
1
mutant enzyme E83A, oxaloacetate-forming activity in the presence of 2 mM Mn2+
10.6
mutant enzyme D75A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
12.3
wild type enzyme, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
15.5
mutant enzyme D75A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2
29.4
wild type enzyme, oxaloacetate-forming activity in the presence of 2 mM Mn2+
43
wild type enzyme, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
recombinant enzyme
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PCKG_MYCSM
605
0
66944
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71200
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D75A
75% reduced activity
D75N
reduced activity
D75Q
reduced activity
D75S
reduced activity
D78A
severely reduced activity
E83A
severely reduced activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 1 month, 24% loss of activity
4°C, purified recombinant His-tagged enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 2 months, 25% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
pck gene, overexpression in Escherichia coli C41(DE3), sequencing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mukhopadhyay, B.; Concar, E.M.; Wolfe, R.S.
A GTP-dependent vertebrate-type phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis
J. Biol. Chem.
276
16137-16145
2001
Mycolicibacterium smegmatis (Q9AGJ6), Mycolicibacterium smegmatis mc(2)155 (Q9AGJ6)
Manually annotated by BRENDA team
Case, C.L.; Concar, E.M.; Boswell, K.L.; Mukhopadhyay, B.
Roles of Asp75, Asp78, and Glu83 of GTP-dependent phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis
J. Biol. Chem.
281
39262-39272
2006
Mycolicibacterium smegmatis (Q9AGJ6)
Manually annotated by BRENDA team