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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Sorghum bicolor and UniProt Accession P15804
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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
-
crassulacean
-
high-fat
- rubisco
-
anaplerotic
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proliferator-activated
- hepatoma
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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
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glycogenolysis
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photorespiration
- fructose-1,6-bisphosphatase
- carboxylases
-
6-phosphatase
-
hypoglycemic
- oxalacetate
- rubp
-
1,5-bisphosphate
- biotechnology
-
perivenous
- agriculture
- synthesis
-
transphosphorylating
-
photorespiratory
-
1,6-bisphosphatase
The taxonomic range for the selected organisms is: Sorghum bicolor
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
PEPCase
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Phosphoenolpyruvate carboxylase
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Phosphoenolpyruvic carboxylase
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PEPC
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
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-
-
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decarboxylation
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-malate
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the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
lyso-phosphatidic acid
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addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 45% of the control activity
phosphatidic acid
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addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity. Inclusion of D-glucose 6-phosphate or L-malate do not change the effect of phosphatidic acid on PEPC, preincubation of the enzyme with 5 mM phosphoenolpyruvate prior to the addition of phosphatidic acid did not prevent inactivation either. The incubation of phosphatidic acid-inactivated PEPC with protein kinase A does not restore PEPC activity
phosphatidylinositol
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addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity
phosphatidylinositol 4-phosphate
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addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 50% of the control activity
phosphatidylserine
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addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 80% of the control activity
additional information
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phosphatidylcholine and phosphatidylethanolamine have no effect on enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
phosphoenolpyruvate
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desalted extracts from de-embryonated dry seed at pH 8
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.174
phosphoenolpyruvate
DELTAC4, deletion of the last 4 c-terminal amino acids
9.5
phosphoenolpyruvate
DELTAC1, deletion of the last c-terminal amino acid
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.075
L-malate
Sorghum bicolor
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the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the four C-terminal mutant enzymes display varying degrees of PEPC activity in vitro ranging from 23% of wild-type with the modest G961A substitution to only 0.2% for the DELTAC4-truncated form
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
PPC3 is the most abundant isozyme of the developing seed, and of the embryo and the aleurone layer of germinating seeds
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activity and protein level of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
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presence of ammonium increases the phosphorylation state of PEPC and PEPC kinase activity in sorghum leaves, both in light and in the dark
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activity and protein level of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
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presence of ammonium increases PEPC activity and the amount of monoubiquitinated PEPC
extensive transcript abundance of isoform PPC2 throughout the entire life cycle of the seed. SbPPC2 shows maximal transcript abundance at 24-48 h post-imbibition and then decreases
extensive transcript abundance of isoform PPC3 throughout the entire life cycle of the seed. PPC3 is the most abundant isozyme of the developing seed, and of the embryo and the aleurone layer of germinating seeds. PPC3 transcript levels are at maximum at the beginning of seed development, during the period of cellularization
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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activity and proteins levels of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
physiological function
important contribution of the SbPPC4 isogene to the cellularization stage of development (stage I) and during germination
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_SORBI
960
0
108372
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
ubiquitination
phosphoprotein
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C4-PEPC is regulated by phosphorylation by a phosphoenolpyruvate carboxylase kinase, n-butanol leads to the partial inhibition of the C4-PEPC phosphorylation
phosphoprotein
monoubiquitinated isoform PPC2 is phosphorylated at its conserved N-terminal seryl phosphorylation site, i.e. Ser13
phosphoprotein
monoubiquitinated isoform PPC3 is phosphorylated at its conserved N-terminal seryl phosphorylation site, i.e. Ser7
ubiquitination
isoform PPC2 is monoubiquitinated in vivo, probybly at at the conserved residue Lys630
ubiquitination
isoform PPC3 is monoubiquitinated in vivo, probably at at the conserved residue Lys624
ubiquitination
isooform PPC4 is monoubiquitinated in vivo
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
delataC1
deletion of the last c-terminal amino acid. kcat: 9.5/sec (phosphoenolpyruvate),12.6% of wild type catalytic activity
delataC4
deletion of the last 4 c-terminal amino acids. kcat: 0.174/sec (phosphoenolpyruvate), 0.14% wild type catalytic activity
G961A
kcat: 17.4/sec (phosphoenolpyruvate), 24.3% of wild type catalytic activity
G961V
kcat: 7.2/sec (phosphoenolpyruvate), 8.5% of wild type catalytic activity
additional information
it is shown that even a modest, neutral alteration of the PEPC C-terminal hydrogen atom side chain is detrimental to enzyme function
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned as a Histag-fusion protein in an Escherichia coli PEPC- (Ppc-) strain
phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase are overexpressed in Escherichia coli concurrently to improve the production of succinate. This coexpression system is also applied to mutant strains of Escherichia coli strategically designed by inactivating the competing pathways of succinate formation. Coexpression of phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase is effective in depleting pyruvate accumulation and increasing the production of metabolites
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase are overexpressed in Escherichia coli concurrently to improve the production of succinate. This coexpression system is also applied to mutant strains of Escherichia coli strategically designed by inactivating the competing pathways of succinate formation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pacquit, V.; Santi, S.; Cretin, C.; Bui, V.L.; Vidal, J.; Gadal, P.
Production and properties of recombinant C3-type phosphoenolpyruvate carboxylase from Sorghum vulgare: in vitro phosphorylation by leaf and root PyrPC protein serine kinase
Biochem. Biophys. Res. Commun.
197
1415-1423
1993
Sorghum bicolor
Nhiri, M.; Bakrim, N.; El Hachimi-Messouak, Z.; Echevarria, C.; Vidal, J.
Posttranslational regulation of phosphoenolpyruvate carboxylase during germination of Sorghum seeds: influence of NaCl and L-malate
Plant Sci.
151
29-37
2000
Sorghum bicolor
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Lin, H.; San, K.Y.; Bennett, G.N.
Effect of Sorghum vulgare phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase coexpression on succinate production in mutant strains of Escherichia coli
Appl. Microbiol. Biotechnol.
67
515-523
2005
Sorghum bicolor
Xu, W.; Ahmed, S.; Moriyama, H.; Chollet, R.
The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall catalysis: mutagenesis and truncation of GLY-961 in the sorghum C4 leaf isoform
J. Biol. Chem.
281
17238-17245
2006
Sorghum bicolor (P15804)
Monreal, J.A.; Lopez-Baena, F.J.; Vidal, J.; Echevarria, C.; Garcia-Maurino, S.
Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase
J. Exp. Bot.
61
2819-2827
2010
Sorghum bicolor
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
Ruiz-Ballesta, I.; Baena, G.; Gandullo, J.; Wang, L.; She, Y.M.; Plaxton, W.C.; Echevarria, C.
New insights into the post-translational modification of multiple phosphoenolpyruvate carboxylase isoenzymes by phosphorylation and monoubiquitination during sorghum seed development and germination
J. Exp. Bot.
67
3523-3536
2016
Sorghum bicolor (C5X951), Sorghum bicolor (C5XYZ9), Sorghum bicolor (C5YK81)
Arias-Baldrich, C.; de la Osa, C.; Bosch, N.; Ruiz-Ballesta, I.; Monreal, J.A.; Garcia-Maurino, S.
Enzymatic activity, gene expression and posttranslational modifications of photosynthetic and non-photosynthetic phosphoenolpyruvate carboxylase in ammonium-stressed sorghum plants
J. Plant Physiol.
214
39-47
2017
Sorghum bicolor
El Omari, R.; Ben Mrid, R.; Chibi, F.; Nhiri, M.
Involvement of phosphoenolpyruvate carboxylase and antioxydants enzymes in nitrogen nutrition tolerance in Sorghum bicolor plants
Russ. J. Plant Physiol.
63
719-726
2016
Sorghum bicolor
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