Information on EC 4.1.1.49 - phosphoenolpyruvate carboxykinase (ATP)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.49
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxykinase (ATP)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
-
Carbon fixation in photosynthetic organisms
-
-
Citrate cycle (TCA cycle)
-
-
gluconeogenesis I
-
-
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pyruvate metabolism
-
-
superpathway of glyoxylate cycle and fatty acid degradation
-
-
C4 and CAM-carbon fixation
-
-
gluconeogenesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9073-94-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Alternanthera ficoides
-
-
-
Manually annotated by BRENDA team
Anaerobiospirillum succiniproducens
-
-
-
Manually annotated by BRENDA team
pineapple
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
phaeophyte, kelp
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
no activity in Hordeum vulgare
barley
-
-
Manually annotated by BRENDA team
no activity in Saccharum officinarum
sugar cane
-
-
Manually annotated by BRENDA team
no activity in Sorghum bicolor
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pea, L. cv. Onward
-
-
Manually annotated by BRENDA team
laboratory clone 3D7
SwissProt
Manually annotated by BRENDA team
cherry
-
-
Manually annotated by BRENDA team
No. 7
-
-
Manually annotated by BRENDA team
No. 7
-
-
Manually annotated by BRENDA team
strain ATCC27210[T]
UniProt
Manually annotated by BRENDA team
strain ATCC27210[T]
UniProt
Manually annotated by BRENDA team
strain TH1
Uniprot
Manually annotated by BRENDA team
strain TH1
Uniprot
Manually annotated by BRENDA team
marine diatom
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
Tul O strain
-
-
Manually annotated by BRENDA team
marine macroscopic green alga
-
-
Manually annotated by BRENDA team
Steudel Jacklin Sunrise Brand
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
lack of phosphoenolpyruvate carboxykinase leads to activation of AMP-activated protein kinase, which inhibits cAMP-induced steroidogenic gene promoter activity and gene expression
physiological function
-
the enzyme is required for steroidogenesis in testicular Leydig cells
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + (E)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
show the reaction diagram
ADP + (Z)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
show the reaction diagram
ADP + phosphoenolpyruvate + CO2
?
show the reaction diagram
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
ATP + aspartate
ADP + alanine + CO2
show the reaction diagram
-
-
-
?
ATP + oxaloacetate
?
show the reaction diagram
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
show the reaction diagram
CTP + oxaloacetate
CDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
15% of the activity with ATP
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
TTP + oxaloacetate
TDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
16% of the activity with ATP
-
-
-
UTP + oxaloacetate
UDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
20% of the activity with ATP
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate + CO2
?
show the reaction diagram
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
ATP + oxaloacetate
?
show the reaction diagram
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation
Zn2+
-
61% of the activation with Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
10 mM, slight
2,3-Butanedione
-
phosphoenolpyruvate, ADP and Mn2+, alone or in combination protect against inactivation
3-Mercaptopicolinic acid
5,5'-dithiobis(2-nitrobenzoate)
-
-
D-fructose 1,6-bisphosphate
D-fructose 6-phosphate
dihydroxyacetone phosphate
Fluorescein mercuric acetate
fructose 1,6-bisphosphate
-
-
fructose 6-phosphate
-
-
Glycerate 3-phosphate
IDP
-
inhibits exchange reaction with ATP or GTP
iodoacetamide
-
less than 10% inhibition
KCl
-
67 mM, slight
malate
mercuribenzoate
-
0.1 mM
MnCl2
-
excess ogf MnCl2 over ATP is inhibitory
NEM
-
less than 10% inhibition
o-Iodobenzoate
-
0.2 mM , 50% inhibition
o-Iodosobenzoate
-
0.5 mM, 50% inhibition
oxalate
p-chloromercuribenzenesulfonate
p-chloromercuribenzoate
Phenylglyoxal
-
phosphoenolpyruvate, ADP and Mn2+, alone or in combination protect against inactivation. Modification of only two of the three to four reactive arginine residues per enzyme subunit is responsible for inactivation
quinolinic acid
-
1 mM, complete inhibition of decarboxylation
additional information
presence of inorganic phosphate strongly reduces expression of PPCK1 and PPCK2 transcripts
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
slight activation of decarboxylation
acetyl-CoA
-
-
D-Glucose-6-phosphate
dithiothreitol
-
activates
fumarate
-
slight activation of decarboxylation
L-fructose 1,6-bisphosphate
-
-
malate
-
slight activation of decarboxylation
succinate
-
slight activation of decarboxylation
additional information
NH4+, NO3- and K+ do not affect PPCK transcript abundance. Sucrose is required for the induction of PPCK2, but not PPCK1, by inorganic phosphate starvation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059 - 0.0085
(Z)-3-fluorophosphoenolpyruvate
0.01 - 44
ADP
0.0011 - 2.3
ATP
0.02 - 47
CO2
0.009 - 26
HCO3-
0.039
MgADP-
-
-
0.01 - 0.345
Mn2+
0.017 - 2.03
MnADP-
0.016 - 0.067
MnATP2-
0.066 - 5.2
oxalacetate
0.014 - 2
oxaloacetate
0.035 - 8
phosphoenolpyruvate
additional information
additional information
-
MnATP2- as substrate, for S252A mutant Km above 3000 microM
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 1.1
(Z)-3-fluorophosphoenolpyruvate
13 - 62
ADP
3 - 38
ATP
0.32 - 65
oxalacetate
0.08 - 0.85
oxaloacetate
0.014 - 63
phosphoenolpyruvate
additional information
additional information
Saccharomyces cerevisiae
-
kcat for oxalacetate as a substrate is above 19 1/s for S252A mutant in the phosphoenolpyruvate formation direction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
130 - 1800
ADP
13
180 - 1300
ATP
4
11
phosphoenolpyruvate
Escherichia coli
-
at pH 7.0 and 37°C
51
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
Fluorescein mercuric acetate
-
-
0.004 - 0.07
malate
0.2
o-Iodobenzoate
-
-
0.5
o-Iodosobenzoate
-
-
0.0025
p-chloromercuribenzenesulfonate
-
-
0.007
p-chloromercuribenzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.31
-
in 50 mM Tris-HCl (pH 8.0) and 5 mM dithiothreitol, at 55°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
carboxylation
6.1
-
exchange reaction between 14CO2 and the beta-carboxyl group of oxaloacetate
6.6
-
assay in the pyruvate kinase-like reaction
7.3
-
decarboxylation
7.5
-
phosphoenolpyruvate formation, Tris-HCl buffer
8
-
decarboxylation
8.3
-
phosphoenolpyruvate formation
additional information
expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
ratio of the two values is pH-dependent and a calibration curve is constructed measuring the fluorescence of free BCECF over the pH range 4-8
5.3 - 7.5
-
pH 5.3: about 30% of maximal activity, pH 7.5: about 25% of maximal activity, oxaloacetate formation
6 - 8.5
6.3 - 9.3
-
pH 6.3: about 35% of maximal activity, pH 9.3: about 30% of maximal activity, phosphoenolpyruvate formation
additional information
-
it is shown that Mn2+ affinity increases as the pH increases
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 53
-
in presence of phosphoenolpyruvate and MnCl2, 50% loss of enzyme activity at 52.5°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is present in the companion cells of the adaxial phloem of minor veins, the internal and external phloem of vascular bundles in petioles and stems, the phloem in roots and the eextra-fascicular phloem in leaves, cotyledons, petioles and stems
Manually annotated by BRENDA team
-
the enzyme is present in the companion cells of the adaxial phloem of minor veins, the internal and external phloem of vascular bundles in petioles and stems, the phloem in roots and the eextra-fascicular phloem in leaves, cotyledons, petioles and stems
Manually annotated by BRENDA team
additional information
-
OsPPCK1 are highly expressed in roots and at low levels in other organs; OsPPCK3 is highly expressed in roots and at low levels in other organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE