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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Ricinus communis and UniProt Accession A6YM33
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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
-
proliferator-activated
- hepatoma
-
nadp-malic
-
tricarboxylic
- ribulose
-
lipogenesis
- dikinase
-
lipogenic
- sorghum
-
periportal
- ribulose-1,5-bisphosphate
-
anti-diabetic
- orthophosphate
-
glycogenolysis
-
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: Ricinus communis
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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-
-
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CP21
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-
-
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CP28
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-
-
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CP46
-
-
-
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PEP carboxylase
PEPC
PEPCase
-
-
-
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Phosphoenolpyruvate carboxylase
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-
-
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Phosphoenolpyruvic carboxylase
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-
-
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PEP carboxylase
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-
-
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PEPC
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
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decarboxylation
-
-
-
-
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
-
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 + HCO3-
phosphate + oxaloacetate
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-
-
-
?
additional information
?
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recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
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-
?
additional information
?
-
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BTPC tightly interacts with co-expressed PTPC to form the allosterically-desensitized class-2 PEPC heteromeric complex
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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
additional information
?
-
recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
absolutely dependent on, PPC4 exhibits a 4fold higher specific activity with saturating (10mM) Mg2+ relative to Mn2+
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
2 mM, 65% decreases of activity of PEPC1 at pH 7.3, 13% decrease in activity of PEPC2 at pH 8
L-Asp
-
2 mM, 95% decreases of activity of PEPC1 at pH 7.3, 49% decrease in activity of PEPC2 at pH 8
L-Glu
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 22% decrease in activity of PEPC2 at pH 8
aspartate
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IC50 of phospho-PEPC1: 0.35 mM, IC50 of dephospho-PEPC1: 0.32 mM
aspartate
-
IC50 of phospho-PEPC2: 2.6 mM, IC50 of dephospho-PEPC2: 4.5 mM, enzyme form PEPC2
glutamate
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IC50 of phospho-PEPC2: 4.1 mM, IC50 of dephospho-PEPC2: 7.0 mM, enzyme form PEPC2
malate
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 59% decrease in activity of PEPC1 at pH 8
malate
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IC50 of phospho-PEPC2: 0.57 mM, IC50 of dephospho-PEPC2: 1.47 mM, enzyme form PEPC2
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 6-phosphate
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2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 1-phosphate
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2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
fructose 6-phosphate
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2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.27fold increase in activity of PEPC1 at pH 8
glucose 1-phosphate
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2 mM, 1.64fold increase of activity of PEPC1 at pH 7.3, 1.07fold increase in activity of PEPC1 at pH 8
malate
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2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 6-phosphate
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2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 6-phosphate
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2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.18fold increase in activity of PEPC1 at pH 8
glycerol 3-phosphate
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2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
glycerol 3-phosphate
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2 mM, 1.83fold increase of activity of PEPC1 at pH 7.3, 1.16fold increase in activity of PEPC1 at pH 8
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
pH 6.5: about 35% of maximal activity, pH 9.5: about 75% of maximal activity, PEPC2
7 - 9.6
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pH 7.0: about 60% of maximal activity, pH 9.5: about 90% of maximal activity, PEPC1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
BTPC is present in leaf buds and young expanding leaves, but undetectable in fully expanded leaves
additional information
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BTPC is abundant in the inner integument, cotyledon, and endosperm of developing seeds
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
plant-type and bacterial-type phosphoenolpyruvate carboxylase (PEPC) interact in vivo as a class-2 PEPC complex that associates with the surface of mitochondria
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the plant-type phosphoenolpyruvate carboxylase-containing class-1 phosphoenolpyruvate carboxylase is entirely cytosolic
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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BTPC and thus class-2 PEPC up-regulation is a distinctive feature of rapidly growing and/or biosynthetically active tissues that require a large anaplerotic flux from phosphoenolpyruvate to replenish tricarboxylic acid cycle C-skeletons being withdrawn for anabolism
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). A6YM33_RICCO
1052
0
118462
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
107000
118000
410000
64000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterooctamer
homotetramer
octamer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
ubiquitination
-
PTPC of castor oil seeds is inhibited by monoubiquitination at Lys-628 during germination
phosphoprotein
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Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases KM-value of PEPC2 for phosphoenolpyruvate and sensitivity to L-malate, glutamic acid, and aspartic acid inhibition. Phosphorylation of subunit p107 is promoted during development of Ricinus communis but disappears during desiccation. The p107 stage VII becomes fully dephosphorylated in plants 48 h following excision of Ricinus communis pods or following 72 h of dark treatment of intact plants
phosphoprotein
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Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases PEPC1 activity at pH 7.3 by decreasing its KM for phosphoenolpyruvate and sensitivity to L-malate inhibition, while enhancing glucose 6-phosphate activation
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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phosphorylation at Ser425 is promoted during seed development, Ser425 phosphorylation results in significant bacterial-type phosphoenolpyruvate carboxylase inhibition
phosphoprotein
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PTPC of castor oil seeds is activated by phosphorylation at Ser-11 during endosperm development
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S425A
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the mutant shows strongly increased Km values compared to the wild type enzyme
S425A/S451D
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the mutant shows strongly increased Km values compared to the wild type enzyme
S451D
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the mutant shows strongly increased Km values compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
55
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% (v/v) glycerol, the final PPC4 preparation proves difficult to store as it slowly loses activity and is completely inactivated when rapidly thawed after freezing in liquid N2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Superose-6 gel filtration, and Superdex 200 gel filtration
Ni2+ affinity resin column chromatography, Superdex 200 gel filtration, and Superose-6 gel filtration
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Ni2+ affinity resin column chromatography, Superdex-200 gel filtration, and Superose-6 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blonde, J.D.; Plaxton, W.C.
Structural and kinetic properties of high and low molecular mass phosphoenolpyruvate carboxylase isoforms from the endosperm of developing castor oilseeds
J. Biol. Chem.
278
11867-11873
2003
Ricinus communis
Tripodi, K.E.; Turner, W.L.; Gennidakis, S.; Plaxton, W.C.
In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase isoforms in endosperm of developing castor oil seeds
Plant Physiol.
139
969-978
2005
Ricinus communis
OLeary, B.; Rao, S.K.; Kim, J.; Plaxton, W.C.
Bacterial-type phosphoenolpyruvate carboxylase (PEPC) functions as a catalytic and regulatory subunit of the novel class-2 PEPC complex of vascular plants
J. Biol. Chem.
284
24797-24805
2009
Ricinus communis (A6YM33)
OLeary, B.; Rao, S.; Plaxton, W.
Phosphorylation of bacterial-type phosphoenolpyruvate carboxylase at Ser425 provides a further tier of enzyme control in developing castor oil seeds
Biochem. J.
433
65-74
2011
Ricinus communis
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
OLeary, B.; Fedosejevs, E.T.; Hill, A.T.; Bettridge, J.; Park, J.; Rao, S.K.; Leach, C.A.; Plaxton, W.C.
Tissue-specific expression and post-translational modifications of plant- and bacterial-type phosphoenolpyruvate carboxylase isozymes of the castor oil plant, Ricinus communis L
J. Exp. Bot.
62
5485-5495
2011
Ricinus communis
Hill, A.T.; Ying, S.; Plaxton, W.C.
Phosphorylation of bacterial-type phosphoenolpyruvate carboxylase by a Ca2+-dependent protein kinase suggests a link between Ca2+ signalling and anaplerotic pathway control in developing castor oil seeds
Biochem. J.
458
109-118
2014
Ricinus communis
Dalziel, K.J.; OLeary, B.; Brikis, C.; Rao, S.K.; She, Y.M.; Cyr, T.; Plaxton, W.C.
The bacterial-type phosphoenolpyruvate carboxylase isozyme from developing castor oil seeds is subject to in vivo regulatory phosphorylation at serine-451
FEBS Lett.
586
1049-1054
2012
Ricinus communis
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