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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Clostridium perfringens and UniProt Accession Q8XLE8

for references in articles please use BRENDA:EC4.1.1.31
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.31 phosphoenolpyruvate carboxylase
IUBMB Comments
This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
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This record set is specific for:
Clostridium perfringens
UNIPROT: Q8XLE8
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The taxonomic range for the selected organisms is: Clostridium perfringens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pepck, phosphoenolpyruvate carboxykinase, pepc, phosphoenolpyruvate carboxylase, pepcase, pep carboxylase, c4 pepc, pepc1, phosphoenol pyruvate carboxylase, pep-carboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
archaeal-type phosphoenolpyruvate carboxylase
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Carboxylase, phosphopyruvate (phosphate)
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CP21
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CP28
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CP46
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PEP carboxylase
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PEPC
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PEPCase
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Phosphoenolpyruvate carboxylase
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Phosphoenolpyruvic carboxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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decarboxylation
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SYSTEMATIC NAME
IUBMB Comments
phosphate:oxaloacetate carboxy-lyase (adding phosphate; phosphoenolpyruvate-forming)
This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9067-77-0
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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
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Mg2+
required for activity, PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Mn2+
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-Asp
L-Asp competitively inhibits the enzyme with respect to the substrate, Mg2+-phosphoenolpyruvate
malonate
weak inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
phosphoenolpyruvate
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH buffer (pH 7.2), at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-Asp
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH buffer (pH 7.2), at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
X-ray crystallography, analytical ultracentrifugation, or sedimentation velocity analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.25-1.5 M sodium malonate, pH 7.0, as precipitant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dharmarajan, L.; Kraszewski, J.L.; Mukhopadhyay, B.; Dunten, P.W.
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate
Proteins
79
1820-1829
2011
Clostridium perfringens (Q8XLE8), Clostridium perfringens
Manually annotated by BRENDA team