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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Escherichia coli and UniProt Accession P00864
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4.1.1.31 phosphoenolpyruvate carboxylaseIUBMB 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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Word Map
- 4.1.1.31
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gluconeogenesis
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gluconeogenic
- malate
- co2
- hepatocytes
- glucose-6-phosphatase
- glycogen
- g6pase
- triglyceride
- maize
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malic
- camp
- glucocorticoid
- hyperglycemia
- adipose
- fructose
- peroxisome
- glucagon
- glucokinase
- mesophyll
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crassulacean
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high-fat
- rubisco
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anaplerotic
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proliferator-activated
- hepatoma
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nadp-malic
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tricarboxylic
- ribulose
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lipogenesis
- dikinase
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lipogenic
- sorghum
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periportal
- ribulose-1,5-bisphosphate
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anti-diabetic
- orthophosphate
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glycogenolysis
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photorespiration
- fructose-1,6-bisphosphatase
- carboxylases
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6-phosphatase
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hypoglycemic
- oxalacetate
- rubp
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1,5-bisphosphate
- biotechnology
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perivenous
- agriculture
- synthesis
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transphosphorylating
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photorespiratory
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1,6-bisphosphatase
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
Phosphoenolpyruvic carboxylase
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Phosphoenolpyruvate carboxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
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decarboxylation
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PATHWAY SOURCE
PATHWAYS
KEGG
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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
9067-77-0
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
phosphoenolpyruvate
wild type enzyme, and mutant enzyme Arg703Gly/Arg704Gly
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
a Propionibacterium freudenreichii strain expressing PepC grows significantly faster, consumes more glycerol, and produces propionate to a higher final titer at a faster rate. The strain also produces significantly more propionate from glucose under elevated CO2 partial pressure
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, crystal structure of the enzyme complexed with Mn2+, the phosphoenolpyruvate analog 3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-prepenoate and an allosteric inhibitor, aspartate, determined at 2.35 A resolution
three-dimensional structure of the enzyme complexed with the allosteric inhibitor L-Asp, determined by X-ray diffraction at 2.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R438C
Arg438Cys has an increased tendency to dissociate into dimers. Mutant enzyme Arg703Gly shows a 5fold decreased turnover number compared to the wild type enzyme
R703G/R703G
mutant enzyme Arg703Gly/Arg704Gly shows a 20fold decreased turnover number compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli DH5alpha. Knock-out as well as over-expression mutants are constructed and characterized. Knocking out phosphoenolpyruvate carboxylase decreases the maximum cell density by 14% and increases the acetate excretion by 7%. Over-expression of phosphoenolpyruvate carboxylase increases the maximum cell dry weight by 91%. No acetate excretion is detected at these increased cell densities
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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elevated acetate concentrations have an inhibitory effect on growth rate and recombinant protein yield, and thus elimination of acetate formation is an important aim towards industrial production of recombinant proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wohl, R.C.; Markus, G.
Phosphoenolpyruvate carboxylase of Escherichia coli
J. Biol. Chem.
247
5785-5792
1972
Escherichia coli, Escherichia coli B / ATCC 11303
Yoshinaga, T.; Teraoka, H.; Izui, K.; Katsuki, H.
Molecular properties of phosphoenolpyruvate carboxylase of Escherichia coli W
J. Biochem.
75
913-924
1974
Escherichia coli
Ishijima, S.; Fujita, N.; Sabe, H.; Izui, K.; Katsuki, H.
Improved method for large scale purification of the phosphoenolpyruvate carboxylase of Escherichia coli K-12
J. Gen. Appl. Microbiol.
30
27-33
1984
Escherichia coli
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Andreo, C.S.; Gonzalez, D.H.; Iglesias, A.A.
Higher plant phosphoenolpyruvate carboxylase
FEBS Lett.
213
1-8
1987
[Brevibacterium] flavum, Crassula argentea, Escherichia coli, Embryophyta
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Gold, E.W.; Smith, T.E.
Escherichia coli phosphoenolpyruvate carboxylase. Effect of allosteric inhibitors on the kinetic parameters and sedimentation behavior
Arch. Biochem. Biophys.
164
447-455
1974
Escherichia coli
Kai, Y.; Matsumura, H.; Inoue, T.; Terada, K.; Nagara, Y.; Yoshinaga, T.; Kihara, A.; Tsumura, K.; Izui, K.
Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition
Proc. Natl. Acad. Sci. USA
96
823-828
1999
Escherichia coli (P00864), Escherichia coli
Matsumura, H.; Xie, Y.; Shirakata, S.; Inoue, T.; Yoshinaga, T.; Ueno, Y.; Izui, K.; Kai, Y.
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases
Structure
10
1721-1730
2002
Escherichia coli (P00864), Escherichia coli, Zea mays (P04711), Zea mays
De Maeseneire, S.L.; De Mey, M.; Vandedrinck, S.; Vandamme, E.J.
Metabolic characterisation of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures
Biotechnol. Lett.
28
1945-1953
2006
Escherichia coli
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