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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Chlamydomonas reinhardtii and UniProt Accession Q6R2V6
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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
-
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
-
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: Chlamydomonas reinhardtii
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
PEPC
PEPCase
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Phosphoenolpyruvate carboxylase
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Phosphoenolpyruvic carboxylase
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PEP carboxylase
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PEPC
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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
Phosphoenolpyruvate + CO2
?
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key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
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?
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
Phosphoenolpyruvate + CO2
?
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key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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CrPpc1/2 polypeptide levels are up-regulated as the initial supply of NH4Cl decreases from 10 to 0.5 mM. However, within 5 h after re-supply of 10 mM NH4Cl to the N-deficient cells, the CrPpc1/2 levels reverts back nearly to those observed in high-N grown cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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PEPC is involved in atmospheric CO2 fixation, C/N interaction and anaplerotic C-flux, energy supply for symbiotic bacteria, carbon storage in cell vacuoles, root malate/citrate excretion for abiotic stress acclimation, seed germination, seed development, and cell expansion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CAPP2_CHLRE
1221
0
131242
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
111000
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4 * 111000 Determined by: 1D native-PAGE and 2D BN-/SDS-PAGE, combined with immunoblotting
669000
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x * 669000, class-2 PEPC enzyme-forms a high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. Determined by: 1D nativePAGE and 2D BN/SDSPAGE, combined with immunoblotting
additional information
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sequencing of the N-terminus, peptide mapping and immunological data suggest that the catalytic subunit of the enzyme is not related to the prokaryotic enzyme and is only distantly related to higher plant C4 and C3 enzymes
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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isoenzyme PEPC2 is a complex between the PEPC catalytic subunit of MW 100000 Da and other immunologically unrelated polypeptides of 50000-700000 Da
heteromer
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x * 669000, class-2 PEPC enzyme-forms a high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. Determined by: 1D nativePAGE and 2D BN/SDSPAGE, combined with immunoblotting
homotetramer
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4 * 111000 Determined by: 1D native-PAGE and 2D BN-/SDS-PAGE, combined with immunoblotting
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Ppc2, expression in Escherichia coli
a high-molecular-mass isoform, PEPC2, and a low-molecular-mass isoform, PEPC1
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isoform-specific purification of CrPpc1 and CrPpc2 is carried out by affinity-purification of using CrPpc1 and CrPpc2 peptide antibodies
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recombinant His-tagged Ppc1, expression in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rivoal, J.; Plaxton, W.C.; Turpin, D.H.
Purification and characterization of high- and low-molecular-mass isoforms of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtii. Kinetic structural and immunological evidence that the green algal enzyme is distinct from the prokaryotic and higher plant enzymes
Biochem. J.
331
201-209
1998
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CW-15 cc1883
Mamedov, T.G.; Moellering, E.R.; Chollet, R.
Identification and expression analysis of two inorganic C- and N-responsive genes encoding novel and distinct molecular forms of eukaryotic phosphoenolpyruvate carboxylase in the green microalga Chlamydomonas reinhardtii
Plant J.
42
832-843
2005
Chlamydomonas reinhardtii (P81831), Chlamydomonas reinhardtii (Q6R2V6), Chlamydomonas reinhardtii
Moellering, E.R.; Ouyang, Y.; Mamedov, T.G.; Chollet, R.
The two divergent PEP-carboxylase catalytic subunits in the green microalga Chlamydomonas reinhardtii respond reversibly to inorganic-N supply and co-exist in the high-molecular-mass, hetero-oligomeric Class-2 PEPC complex
FEBS Lett.
581
4871-4876
2007
Chlamydomonas reinhardtii
O'Leary, B.; Park, J.; Plaxton, W.C.
The remarkable diversity of plant PEPC (phosphoenolpyruvate carboxylase): recent insights into the physiological functions and post-translational controls of non-photosynthetic PEPCs
Biochem. J.
436
15-34
2011
Arabidopsis thaliana, Beta vulgaris, Brassica napus, Ricinus communis, Chlamydomonas reinhardtii, Citrus sinensis, Glycine max, Helianthus annuus, Hordeum vulgare, Lotus japonicus, Lupinus albus, Solanum lycopersicum, Musa cavendishii, Nicotiana tabacum, Oryza sativa, Solanum tuberosum, Triticum aestivum
Tian, Q.L.; Shi, D.J.; Jia, X.H.; Mi, H.L.; Huang, X.W.; He, P.M.
Recombinant expression and functional analysis of a Chlamydomonas reinhardtii bacterial-type phosphoenolpyruvate carboxylase gene fragment
Biotechnol. Lett.
36
821-827
2014
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii FACHB-479
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