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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q84VW9
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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
-
anaplerotic
-
proliferator-activated
- hepatoma
-
nadp-malic
-
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
-
glycogenolysis
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photorespiration
- fructose-1,6-bisphosphatase
- carboxylases
-
6-phosphatase
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hypoglycemic
- oxalacetate
- rubp
-
1,5-bisphosphate
- biotechnology
-
perivenous
- agriculture
- synthesis
-
transphosphorylating
-
photorespiratory
-
1,6-bisphosphatase
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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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-
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Phosphoenolpyruvate carboxylase
Phosphoenolpyruvic carboxylase
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PEP carboxylase
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PEPC
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Phosphoenolpyruvate carboxylase
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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
KEGG
-
-, -, -, -, -, -, -, -, -, -, -
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
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
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-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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not inhibited by phosphatidic acid, phosphatidylinositol, phosphatidylinositol 4-phosphate, lyso-phosphatidic acid, phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
transcripts accumulate to higher levels in roots compared to shoots
additional information
transcripts accumulate to higher levels in roots compared to shoots, PPC3 is the main PEPC isoform expressed in Arabidopsis thaliana roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
additional information
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
additional information
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
additional information
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
an isoform PPC3 mutant has a growth-arrest phenotype and is affected in phosphate and salt-stress responses
physiological function
physiological function
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BTPC accelerates the metabolic flow for the synthesis of storage substances during pollen maturation
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
physiological function
a double mutant lacking both isoforms Ppc1/Ppc2 exhibits a severe growth-arrest phenotype. The Ppc1/Ppc2 mutant accumulates more starch and sucrose than wild-type plants when seedlings are grown under normal conditions. Decreased PEPC activity in the mutant greatly reduces the synthesis of malate and citrate and severely suppresses ammonium assimilation. Nitrate levels in the double mutant are significantly lower than those in wild-type plants due to the suppression of ammonium assimilation. Starch and sucrose accumulation can be prevented and nitrate levels can be maintained by supplying the Ppc1/Ppc2 mutant with exogenous malate and glutamate
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). CAPP3_ARATH
968
0
110160
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
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purified PPC1 is phosphorylated at Ser-11, in vivo phosphorylation of isoform PPC1 during phosphate stress also activates this enzyme at pH 7.3 by significantly lowering its Km(phosphoenolpyruvate) value and sensitivity to inhibition by L-malate and L-Asp, while increasing its activation by D-glucose-6-phosphate
phosphoprotein
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the phosphoenolpyruvate carboxylase kinase gene product PPCk1 is responsible for leaf PEPC phosphorylation
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
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PEPC activity at pH 7.0 is approximately 50% of that occurring at pH 8.5
701501
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Sepharose column chromatography, Fractogel EMD DEAE-650 colum chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli with an N-terminal His-tag
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
BTPC expression initiates after the last mitosis before pollen germination
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sanchez, R.; Flores, A.; Cejudo, F.J.
Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress
Planta
223
901-909
2006
Arabidopsis thaliana (Q5GM68), Arabidopsis thaliana (Q84VW9), Arabidopsis thaliana (Q8GVE8), Arabidopsis thaliana (Q9MAH0)
Dharmarajan, L.; Kraszewski, J.L.; Mukhopadhyay, B.; Dunten, P.W.
Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase
Acta Crystallogr. Sect. F
65
1193-1196
2009
Arabidopsis thaliana
Meimoun, P.; Gousset-Dupont, A.; Lebouteiller, B.; Ambard-Bretteville, F.; Besin, E.; Lelarge, C.; Mauve, C.; Hodges, M.; Vidal, J.
The impact of PEPC phosphorylation on growth and development of Arabidopsis thaliana: molecular and physiological characterization of PEPC kinase mutants
FEBS Lett.
583
1649-1652
2009
Arabidopsis thaliana
Monreal, J.; McLoughlin, F.; Echevarra, C.; Garca-Maurio, S.; Testerink, C.
Phosphoenolpyruvate carboxylase from C4 leaves is selectively targeted for inhibition by anionic phospholipids
Plant Physiol.
152
634-638
2010
Arabidopsis thaliana, Sorghum bicolor, Zea mays
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
Igawa, T.; Fujiwara, M.; Tanaka, I.; Fukao, Y.; Yanagawa, Y.
Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants
BMC Plant Biol.
10
200
2010
Arabidopsis thaliana, Lilium longiflorum
Shi, J.; Yi, K.; Liu, Y.; Xie, L.; Zhou, Z.; Chen, Y.; Hu, Z.; Zheng, T.; Liu, R.; Chen, Y.; Chen, J.
Phosphoenolpyruvate carboxylase in Arabidopsis leaves plays a crucial role in carbon and nitrogen metabolism
Plant Physiol.
167
671-681
2015
Arabidopsis thaliana (Q5GM68), Arabidopsis thaliana (Q9MAH0)
Feria, A.B.; Bosch, N.; Sanchez, A.; Nieto-Ingelmo, A.I.; de la Osa, C.; Echevarria, C.; Garcia-Maurino, S.; Monreal, J.A.
Phosphoenolpyruvate carboxylase (PEPC) and PEPC-kinase (PEPC-k) isoenzymes in Arabidopsis thaliana role in control and abiotic stress conditions
Planta
244
901-913
2016
Arabidopsis thaliana (Q84VW9), Arabidopsis thaliana
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