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Information on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP) and Organism(s) Rattus norvegicus and UniProt Accession P07379
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4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)IUBMB Comments
ITP can act as phosphate donor.
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Word Map
- 4.1.1.32
- biliary
- cirrhosis
-
gluconeogenesis
- autoantigens
- autoimmune
-
gluconeogenic
- autoantibody
- epitope
-
lipoylated
-
antimitochondrial
- camp
- glucocorticoid
- bile
-
immunodominant
- malate
-
malic
-
autoreactive
- cholangitis
-
intrahepatic
-
lipoic
-
autoepitope
-
glyceroneogenesis
-
dibutyryl
-
6.4.1.1
-
anaplerotic
-
3-mercaptopicolinic
-
2.7.1.40
-
bt2camp
-
pbc-specific
-
fto-2b
- oxalacetate
- 2-oxo-acid
-
ama-positive
- dihydrolipoamide
-
self-tolerance
- drug development
- synthesis
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pdc-e2, pepck-c, pep carboxykinase, p-enolpyruvate carboxykinase, phosphoenolpyruvate carboxykinase (gtp), pepck-m, pep-carboxykinase, phosphopyruvate carboxylase, phosphopyruvate carboxykinase, gtp:oxaloacetate carboxy-lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxykinase, phosphopyruvate (guanosine triphosphate)
-
-
-
-
oxaloacetate kinase (decarboxylating, GDP)
-
-
-
-
P-enolpyruvate carboxykinase
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxylase
-
-
-
-
PEPCK
phosphoenolpyruvate carboxykinase
Phosphoenolpyruvate carboxylase
-
-
-
-
phosphoenolpyruvate carboxylase (GTP)
-
-
-
-
phosphoenolpyruvic carboxykinase
-
-
-
-
phosphoenolpyruvic carboxykinase (GTP)
-
-
-
-
phosphoenolpyruvic carboxykinase (inosine triphosphate)
-
-
-
-
Phosphoenolpyruvic carboxylase
-
-
-
-
phosphoenolpyruvic carboxylase (GTP)
-
-
-
-
phosphoenolpyruvic carboxylase (inosine triphosphate)
-
-
-
-
phosphopyruvate carboxykinase
-
-
-
-
phosphopyruvate carboxylase
-
-
-
-
phosphopyruvate carboxylase (GTP)
-
-
-
-
PEPCK
-
-
-
-
phosphoenolpyruvate carboxykinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
the enzyme decarboxylates oxaloacetate to form the enolate of pyruvate which is then phosphorylated by MgGTP2- on the enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
GTP:oxaloacetate carboxy-lyase (adding GTP; phosphoenolpyruvate-forming)
ITP can act as phosphate donor.
CAS REGISTRY NUMBER
COMMENTARY
9013-08-5
-
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
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
physiological direction of reaction
-
-
r
GTP + oxaloacetate
?
-
induced by a combination of dibutyryl cAMP, theophylline, and dexamethasone
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
specifically requires GTP or ITP, structural data of GTP binding
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
catalyzes the rate-limiting step in gluconeogenesis, PEPCK expression and growth arrest may be coordinately regulated
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
primary role is the formation of phosphoenolpyruvate in the first committed step of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
first committed step of gluconeogenesis
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
specifically requires GTP or ITP
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
rate limiting enzyme of gluconeogenesis
-
-
?
additional information
?
-
-
catalyzes bicarbonate-dependent phosphorylation of hydroxylamine
-
-
?
additional information
?
-
-
enzyme catalyzes the phosphorylation of glycolate, thioglycolate, and DL-beta-chloroacetate
-
-
?
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
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
rate limiting enzyme of gluconeogenesis
-
-
?
GTP + oxaloacetate
?
-
induced by a combination of dibutyryl cAMP, theophylline, and dexamethasone
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
catalyzes the rate-limiting step in gluconeogenesis, PEPCK expression and growth arrest may be coordinately regulated
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
primary role is the formation of phosphoenolpyruvate in the first committed step of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
first committed step of gluconeogenesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mn2+
Fe2+
-
Fe2+ alone does not stimulate, Fe2+ + ferroactivator, stimulate in both directions of the reaction
Fe2+
-
0.05 mM FeCl2 and 0.0044 mg/ml ferroactivator, enhance to 3.1times the unstimulated rate. 1.5 mM FeCl2 causes rapid inactivation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-azidoguanosine 5'-triphosphate
-
photoinactivation is caused by formation of an intramolecular cystine disulfide bridge
FeCl2
-
1.5 mM FeCl2 causes rapid inactivation. 0.05 mM FeCl2 and 0.0044 mg/ml ferroactivator, enhance to 3.1times the unstimulated rate
interleukin-10
-
added to cell culture medium in combination with interleukin-1beta, reduces mRNA and enzyme level
-
interleukin-1beta
-
added to cell culture medium in combination with interleukin-10, reduces mRNA and enzyme level
-
quinolinic acid
-
strongly inhibits the enzyme activated by ferroactivator and Fe2+, no inhibition of Mn2+-activated enzyme
2-oxoglutarate
-
in both directions, competitive with respect to oxaloacetate or phosphoenolpyruvate, noncompetitive with respect GTP or Mn2+
additional information
-
vanadate inhibits transcription of the phosphoenolpyruvate carboxykinase gene
-
additional information
-
insulin is a potent dominant repressor of PEPCK gene transcription and causes a rapid decrease of PEPCK mRNA
-
additional information
-
reduced expression of mRNA when cells are cultured in conditioned medium obtained from LPS-stimulated Kupffer cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferroactivator
-
ferroactivator + Fe2+, stimulates both directions of the reaction
-
additional information
-
PEPCK mRNA is elevated in cells cultured at high density, expression is induced by contact inhibition in the presence of serum, at low culture density, dexamethasone induces PEPCK mRNA 5-8fold, at high culture density 2-3fold
-
additional information
-
methylprednisolone induces enzyme expressions via cAMP
-
additional information
-
all-trans-retinoic acid is a transcriptional inducer of the PEPCK-C gene. 9-cis-retinoic acid and all-trans-retinoic acid stimulate PEPCK-C expression in 3T3-442A adipocytes
-
additional information
-
ketogenic diet-fed rats have increased fat mass and phosphoenolpyruvate carboxykinase activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.814
CO2
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
1.194
CO2
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.039
GDP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.07
GDP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.047
GTP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.068
GTP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.052
oxaloacetate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.749
oxaloacetate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.063
phosphoenolpyruvate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.294
phosphoenolpyruvate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
CO2
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
19
CO2
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
1
GDP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
19
GDP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
14
GTP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
54
GTP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
14
oxaloacetate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
54
oxaloacetate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
1
phosphoenolpyruvate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
19
phosphoenolpyruvate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
CO2
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
16
CO2
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
14
GDP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
510
GDP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
270
GTP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
790
GTP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
19
oxaloacetate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
1000
oxaloacetate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
15
phosphoenolpyruvate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
66
phosphoenolpyruvate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
cultured cells in co-culture with lipopolysaccharide stimulated Kupffer cells
-
higher level of PEPCK mRNA is observed in spherical rat primary hepatocytes on EHS-gel than monolayer hepatocytes on type I collagen
-
H4IIEC3 cells, mRNA is 5-10fold elevated in cells cultured at high density compared to low density, KRC-7 cells, an H4IIEC3 subclone, are much more sensitive to growth arrest than its parental cell line
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme loss impairs gluconeogenesis from lactate, lowers plasma glucose, insulin, and triglycerides, reduces hepatic glycogen, and increases glycerol turnover
metabolism
-
approximately a third of gluconeogenesis comes from the enzyme
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). PCKGC_RAT
622
0
69416
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, at 25 ?C in 0.1 M HEPES (pH 7.4) and 12-30% PEG 3350, creating PEPCK-Mn2+, PEPCK-Mn2+-oxaloacetate, PEPCK-Mn2+-oxaloacetate-Mn2+GDP, and PEPCKMn2+-Mn2+GTP crystals
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A467G
PEPCK has a 14fold higher Km value for oxaloacetate than wild type, coupled with a reduction in kcat (26% of wild type), resulting in a reduction in catalytic efficiency by nearly two orders of magnitude (1.9% of wild type). There is little change in the Km for GTP (factor of 1.4), resulting in the catalytic efficiency for GTP decreasing by less than a factor of three. In the reverse reaction, the mutant shows a decrease in the Km value for phosphoenolpyruvate (21% of wild type), a kcat reduced to 5% of the wild type value, and a factor of four reduction in the catalytic efficiency relative to wild type
additional information
additional information
-
enzyme synthesized in presence of the amino acid analogues, canavanine replacing Arg or 5-fluorotryptophan or 6-fluorotryptophan replacing Trp. The canavanine-containing enzyme and the 6-fluorotryptophan-containing enzyme are degraded more rapidly than the enzyme containing all natural amino acids
additional information
-
mechanism of inactivation of PEPCK by Cys-273 modification due to inhibition of a dynamic motion that may occur upon nucleotide binding
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
protein concentration 0.057 mg/ml, glutathione concentration 0.2 mM, stable for at least 3 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in absence of metal ions, under N2, protein concentration 0.5 mg/ml or higher, stable for at least 14 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Uniflow resin column chromatography and P6DG column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of SIRT1 by resveratrol represses transcription of the gene for the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) by deacetylating hepatic nuclear factor 4alpha. Isonicotinamide decreases the level of mRNA for PEPCK-C
-
phenobarbital directly suppresses PEPCK gene expression in spherical hepatocytes on EHS-gel, but not in those on type I collagen. Phenobarbital strongly suppresses cAMP-dependent induction of PEPCK gene expression
-
there is a significant increase of 85% in kidney PEPCK activity of diabetic rats 0.85 units/g tissue/min in comparison to the 0.46 units/g tissue/min of normal controls, treatment of diabetic animals with cinnamaldehyde and glibenclamide for 60 days prevents the increase in PEPCK levels
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
chronic administration of phenobarbital reduces hepatic PEPCK mRNA in streptozotocin-induced diabetic and nondiabetic rats, and phenobarbital reduces blood glucose level in diabetic rats
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Colombo, G.; Carlson, G.M.; Lardy, H.A.
Phosphoenolpyruvate carboxykinase (guanosine triphosphate) from rat liver cytosol. Separation of homogenous forms of the enzyme with high and low activity by chromatography on agarose-hexane-guanosine triphosphate
Biochemistry
17
5321-5329
1978
Rattus norvegicus
Bentle, L.A.; Lardy, H.A.
Phosphoenolpyruvate carboxykinase ferroactivator. Purification and some properties
J. Biol. Chem.
252
1431-1440
1977
Rattus norvegicus
Lewis, C.T.; Haley, B.E.; Carlson, G.M.
Formation of an intramolecular cystine disulfide during the reaction of 8-azidoguanosine 5'-triphosphate with cytosolic phosphoenolpyruvate carboxykinase (GTP) causes inactivation without photolabeling
Biochemistry
28
9248-9255
1989
Rattus norvegicus
Knowles, S.E.; Gunn, J.M.; Reshef, L.; Hanson, R.W.; Ballard, F.J.
Properties of phosphoenolpyruvate carboxykinase (guanosine triphosphate) sythesized in hepatoma cells in the presence of amino acid analogues
Biochem. J.
146
585-593
1975
Rattus norvegicus
Bosch, F.; Hatzoglou, M.; Park, E.A.; Hanson, R.W.
Vanadate inhibits expression of the gene for phosphoenolpyruvate carboxykinase (GTP) in rat hepatoma cells
J. Biol. Chem.
265
13677-13682
1990
Rattus norvegicus
Titheradge, M.A.; Picking, R.A.; Haynes, R.C.
Physiological concentration of 2-oxoglutarate regulate the activity of phosphoenolpyruvate carboxykinase in liver
Biochem. J.
285
767-771
1992
Rattus norvegicus
Ash, D.E.; Emig, F.A.; Chowdhury, S.A.; Satoh, Y.; Schramm, V.L.
Mammalian and avian liver phosphoenolpyruvate carboxykinase. Alternate substrates and inhibition by analogues of oxaloacetate
J. Biol. Chem.
265
7377-7384
1990
Gallus gallus, Rattus norvegicus
Zeitouni, N.; Eubank, D.W.; Lee, A.Q.; Oxford, M.G.; Freeman, T.L.; Mailliard, M.E.; Beale, E.G.
Phosphoenolpyruvate carboxykinase is induced in growth-arrested hepatoma cells
Biochem. Biophys. Res. Commun.
290
1513-1520
2002
Rattus norvegicus
Holyoak, T.; Nowak, T.
Structural investigation of the binding of nucleotide to phosphoenolpyruvate carboxykinase by NMR
Biochemistry
40
11037-11047
2001
Gallus gallus, Rattus norvegicus
Yerkovich, S.T.; Rigby, P.J.; Fournier, P.A.; Olynyk, J.K.; Yeoh, G.C.T.
Kupffer cell cytokines interleukin-1beta and interleukin-10 combine to inhibit phosphoenolpyruvate carboxykinase and gluconeogenesis in cultured hepatocytes
Int. J. Biochem. Cell Biol.
36
1462-1472
2004
Rattus norvegicus
Jin, J.Y.; DuBois, D.C.; Almon, R.R.; Jusko, W.J.
Receptor/gene-mediated pharmacodynamic effects of methylprednisolone on phosphoenolpyruvate carboxykinase regulation in rat liver
J. Pharmacol. Exp. Ther.
309
328-339
2004
Rattus norvegicus
Sullivan, S.M.; Holyoak, T.
Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid
Biochemistry
46
10078-10088
2007
Rattus norvegicus (P07379)
Cadoudal, T.; Glorian, M.; Massias, A.; Fouque, F.; Forest, C.; Benelli, C.
Retinoids upregulate phosphoenolpyruvate carboxykinase and glyceroneogenesis in human and rodent adipocytes
J. Nutr.
138
1004-1009
2008
Rattus norvegicus, Homo sapiens (P35558), Homo sapiens
Ribeiro, L.C.; Chitto, A.L.; Mueller, A.P.; Rocha, J.K.; Castro da Silva, M.; Quincozes-Santos, A.; Nardin, P.; Rotta, L.N.; Ziegler, D.R.; Goncalves, C.A.; Da Silva, R.S.; Perry, M.L.; Gottfried, C.
Ketogenic diet-fed rats have increased fat mass and phosphoenolpyruvate carboxykinase activity
Mol. Nutr. Food Res.
52
1365-1371
2008
Rattus norvegicus
Anand, P.; Murali, K.Y.; Tandon, V.; Murthy, P.S.; Chandra, R.
Insulinotropic effect of cinnamaldehyde on transcriptional regulation of pyruvate kinase, phosphoenolpyruvate carboxykinase, and GLUT4 translocation in experimental diabetic rats
Chem. Biol. Interact.
186
72-81
2010
Rattus norvegicus
Stark, R.; Pasquel, F.; Turcu, A.; Pongratz, R.L.; Roden, M.; Cline, G.W.; Shulman, G.I.; Kibbey, R.G.
Phosphoenolpyruvate cycling via mitochondrial phosphoenolpyruvate carboxykinase links anaplerosis and mitochondrial GTP with insulin secretion
J. Biol. Chem.
284
26578-26590
2009
Rattus norvegicus
Yang, J.; Kong, X.; Martins-Santos, M.E.; Aleman, G.; Chaco, E.; Liu, G.E.; Wu, S.Y.; Samols, D.; Hakimi, P.; Chiang, C.M.; Hanson, R.W.
Activation of SIRT1 by resveratrol represses transcription of the gene for the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) by deacetylating hepatic nuclear factor 4alpha
J. Biol. Chem.
284
27042-27053
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Johnson, T.A.; Holyoak, T.
Increasing the conformational entropy of the Omega-loop lid domain in phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic fidelity
Biochemistry
49
5176-5187
2010
Rattus norvegicus (P07379)
Stark, R.; Guebre-Egziabher, F.; Zhao, X.; Feriod, C.; Dong, J.; Alves, T.C.; Ioja, S.; Pongratz, R.L.; Bhanot, S.; Roden, M.; Cline, G.W.; Shulman, G.I.; Kibbey, R.G.
A role for mitochondrial phosphoenolpyruvate carboxykinase (PEPCK-M) in the regulation of hepatic gluconeogenesis
J. Biol. Chem.
289
7257-7263
2014
Rattus norvegicus
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