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Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase and Organism(s) Zea mays and UniProt Accession P04711

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     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.31 phosphoenolpyruvate carboxylase
IUBMB 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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Zea mays
UNIPROT: P04711
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The taxonomic range for the selected organisms is: Zea mays
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C4 PEPC
-
-
Carboxylase, phosphopyruvate (phosphate)
-
-
-
-
CP21
-
-
-
-
CP28
-
-
-
-
CP46
-
-
-
-
PEP carboxylase
-
-
-
-
PEPCase
-
-
-
-
Phosphoenolpyruvate carboxylase
-
-
-
-
Phosphoenolpyruvic carboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
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 hide
9067-77-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Phosphoenolpyruvate + CO2
?
show the reaction diagram
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Phosphoenolpyruvate + CO2
?
show the reaction diagram
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
key enzyme in fixation of atmospheric CO2 in C4 and crassulacean acid metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphate
-
the enzyme from root is phosphorylated by both mammalian cAMP-dependent protein kinase and maize leaf protein kinase, the phosphorylated enzyme is less sensitive to malate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
competitive
Asp
-
-
aspartate
-
-
ATP
-
competitive
citrate
-
-
Cl-
-
-
L-malate
-
inhibits wild-type enzyme
lyso-phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 45% of the control activity
malate
Mg-(1,2-epoxypropylphosphonic acid) complex
-
-
Mg2+
-
free, non-competitive. Substrate inhibition by Mg-phosphoenolpyruvate is caused by inhibition by high Mg2+ and ionic strength
oxaloacetate
-
-
phosphatidic acid
-
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
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity
phosphatidylinositol 4-phosphate
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 50% of the control activity
phosphatidylserine
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 80% of the control activity
pyruvate
-
-
additional information
-
phosphatidylcholine and phosphatidylethanolamine have no effect on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose 6-phosphate
activates
1,2-Epoxypropylphosphonic acid
-
-
fructose 1,6-bisphosphate
-
weak activation
glucose 1-phosphate
-
weak activation
glucose 6-phosphate
glycerol
-
activates
glycine
His
-
stimulates
phosphoenolpyruvate
-
free, allosteric activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.28 - 1.45
HCO3-
0.047 - 8.7
phosphoenolpyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
-
dark-adapted enzyme form
20.8
-
-
21
-
a light-adapted enzyme form
23.58
-
-
additional information
-
ozone is able to depress PEPc activity. As compared to chambered control atmosphere, significant declines in PEPc activity by circa 26% and 32% are recorded in + 60 and + 80 atmospheres, respectively
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.9 - 8.3
-
-
8
-
root-form PEPC and C4-form PEPC
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
pH 7.0: 90% of maximal activity of the root-form PEPC, 40% of maximal activity of the C4-form PEPC
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
40
-
isoenzyme PC-I
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme partially localizes to membranes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
Oryza sativa plants expressing Zea mays phosphoenolpyruvate carboxylase are taller and have a stronger stalk, wider leaves, and more exuberant root system, with increased photosynthetic enzyme activity and improved yield components
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAPP1_MAIZE
970
0
109297
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
225700
-
sucrose density gradient centrifugation, isoenzyme PC-I
260000
-
enzyme from darkened leaf extract, dimer, gel filtration
270800
-
sucrose density gradient centrifugation, isoenzyme PC-II
285000
-
enzyme from illuminated leaf extract, dimer, gel filtration
340000
-
analytical ultracentrifugation
405000
-
gel filtration
410000
-
enzyme from darkened leaf extract, tetramer, gel filtration
420000
-
enzyme from illuminated leaf extract, tetramer, gel filtration
96000
-
x * 96000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 96000, SDS-PAGE
additional information
-
concentration-dependent dissociation of tetrameric into dimeric forms
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, crystal structure determined at 3.0 A resolution
hanging-drop vapour-diffusion method with PEG 8000 as precipitant at pH 7.5. the crystals belong to space group C222(1), with unit-cell dimensions a = 160.2, b = 175.6, c = 255.5 A, and diffract to 3.2 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D228N
-
reduced apparent affinity for the activator glycine
E229A
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is lower than wild-type value
R183Q
-
mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected
R183Q/R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R226Q
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is significantly higher than that of wild-type enzyme
R231A
-
decreased apparent affinity for the activator glucose 6-phosphate
R232Q
-
decreased apparent affinity for the activator glucose 6-phosphate, reduced apparent affinity for the activator glycine
R372Q
-
mutation results in a marked decrease in sensitivity to glucose 6-phosphate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
15°C, in presence of 1 mM dithiothreitol
4284
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
pH 7.0, in presence of 1 mM dithiothreitol
45
-
50% inactivation after 87 s, isoenzyme PC-I. 50% inactivation after 100 s, isoenzyme PC-II
50
-
50% inactivation after 18 s, isoenzyme PC-I. 50% inactivation after 28 s, isoenzyme PC-II
55
-
50% inactivation after 13 s, isoenzyme PC-I. 50% inactivation after 17 s, isoenzyme PC-II
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by trypsin under non-catalytic conditions, resulting in a truncated enzyme having molecular mass of about 80000 Da. In presence of substrate very little inactivation is observed although the subunit molecular mass is reduced to 90000 Da
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 20% sucrose solution, stable for 14 days
-
-20°C, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a dark-adapted enzyme form and a light-adapted enzyme form
-
isoenzyme PC-I and PC-II
-
recombinant
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a fusion protein, the extra 159 amino acid residues fused at the N-terminus of the enzyme protein have no effect on catalytic and regulatory properties
-
expression in Escherichia coli BL21(DE3)pLysS
-
isozymic forms are encoded by a small gene family
-
root enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kerr, M.W.; Robertson, A.
Properties of phosphoenolpyruvate carboxylase isolated from maize leaves
Biochem. J.
125
34
1971
Zea mays
-
Manually annotated by BRENDA team
Mukerji, S.K.
Corn leaf phosphoenolpyruvate carboxylases. Purification and properties of two isoenzymes
Arch. Biochem. Biophys.
182
343-351
1977
Zea mays
Manually annotated by BRENDA team
Mares, J.; Barthova, J.; Leblova, S.
Purification and properties of phosphoenolpyruvate carboxylase from green leaves of maize
Collect. Czech. Chem. Commun.
44
1835-1840
1979
Zea mays
-
Manually annotated by BRENDA team
Harpster, M.H.; Taylor, W.C.
Maize phosphoenolpyruvate carboxylase. Cloning and characterization of mRNAs encoding isozymic forms
J. Biol. Chem.
261
6132-6136
1986
Zea mays
Manually annotated by BRENDA team
Ogawa, N.; Kai, T.; Yabuta, N.; Izui, K.
Phosphoenolpyruvate carboxylase of maize leaves: an improved method for purification and reduction of the inhibitory effect of malate by ethylene glycol and bicarbonate
Plant Cell Physiol.
38
76-80
1997
Zea mays
-
Manually annotated by BRENDA team
Dong, L.Y.; Masuda, T.; Kawamura, T.; Hata, S.; Izui, K.
Cloning, expression and characterization of a root-form phosphoenolpyruvate carboxylase from Zea mays: comparison with the C4-form enzyme
Plant Cell Physiol.
39
865-873
1998
Zea mays
Manually annotated by BRENDA team
Walker, G.H.; Edwards, G.E.
Tautomerization of oxaloacetate and inhibition of maize leaf phosphoenolpyruvate carboxylase
Phytochemistry
30
751-756
1991
Zea mays
-
Manually annotated by BRENDA team
Mujica-Jimenez, C.; Castellanos-Martinez, A.; Munoz-Clares, R.A.
Studies of the allosteric properties of maize leaf phosphoenolpyruvate carboxylase with the phosphoenolpyruvate analog phosphomycin as activator
Biochim. Biophys. Acta
1386
132-144
1998
Zea mays
Manually annotated by BRENDA team
McNaughton, G.A.L.; Fewson, C.A.; Wilkins, M.B.; Nimmo, H.G.
Purification, oligomerization state and malate sensitivity of maize leaf phosphoenolpyruvate carboxylase
Biochem. J.
261
349-355
1989
Zea mays
Manually annotated by BRENDA team
Dong, L.Y.; Hata, S.; Izui, K.
High-level expression of maize C4-type phosphoenolpyruvate carboxylase in Escherichia coli and its rapid purification
Biosci. Biotechnol. Biochem.
61
545-546
1997
Zea mays
Manually annotated by BRENDA team
Matsumura, H.; Nagata, T.; Terada, M.; Shirakata, S.; Inoue, T.; Yoshinaga, T.; Ueno, Y.; Saze, H.; Izui, K.; Kai, Y.
Crystallization and preliminary X-ray diffraction studies of C4-form phosphoenolpyruvate carboxylase from maize
Acta Crystallogr. Sect. D
55
1937-1938
1999
Zea mays
Manually annotated by BRENDA team
Tovar-Mendez, A.; Munoz-Clares, R.A.
Kinetics of phosphoenolpyruvate carboxylase from Zea mays leaves at high concentration of substrates
Biochim. Biophys. Acta
1546
242-252
2001
Zea mays
Manually annotated by BRENDA team
Maralihalli, G.B.; Bhagwat, A.S.
Limited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylase
Indian J. Biochem. Biophys.
38
361-367
2001
Zea mays
Manually annotated by BRENDA team
Frank, J.; Vater, J.; Holzwarth, J.F.
Kinetics and equilibrium binding of phosphoenolpyruvate to phosphoenolpyruvate carboxylase from Zea mays
Phys. Chem. Chem. Phys.
1
455-461
1999
Zea mays
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Takahashi-Terada, A.; Kotera, M.; Ohshima, K.; Furumoto, T.; Matsumura, H.; Kai, Y.; Izui, K.
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation
J. Biol. Chem.
280
11798-11806
2005
Zea mays
Manually annotated by BRENDA team
Yuan, J.; Sayegh, J.; Mendez, J.; Sward, L.; Sanchez, N.; Sanchez, S.; Waldrop, G.; Grover, S.
The regulatory role of residues 226-232 in phosphoenolpyruvate carboxylase from maize
Photosynth. Res.
88
73-81
2006
Zea mays
Manually annotated by BRENDA team
Leitao, L.; Bethenod, O.; Biolley, J.P.
The impact of ozone on juvenile maize (Zea mays L.) plant photosynthesis: effects on vegetative biomass, pigmentation, and carboxylases (PEPc and Rubisco)
Plant Biol.
9
478-488
2007
Zea mays
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Li, W.C.; Wang, J.; Sun, Y.L.; Ji, S.D.; Guo, S.W.
Morphology and photosynthetic enzyme activity of maize phosphoenolpyruvate carboxylase transgenic rice
Genet. Mol. Res.
14
15572-15576
2015
Zea mays
Manually annotated by BRENDA team