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2'-deoxyguanosine 5'-triphosphate + oxaloacetate
2'-deoxyguanosine 5'-diphosphate + phosphoenolpyruvate + CO2
-
2-deoxyGTP is a less effective substrate than GTP, 2-deoxyGTP binds to enzyme less tight than 2-deoxyGDP
2-deoxyGDP is a less effective substrate than GDP in the reverse reaction
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
dGTP + oxaloacetate
dGDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GDP + (Z)-3-fluorophosphoenolpyruvate + CO2
?
-
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
oxaloacetate + ?
pyruvate + CO2
-
ir
-
?
UDP + phosphoenolpyruvate + CO2
UTP + oxaloacetate
additional information
?
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
the enzyme can also use ATP instead of GTP for oxaloacetate decarboxylation
-
-
ir
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
poor substrate
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
poor activity
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
Modiolus demissus
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
highest activity
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
r
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
-
-
-
-
r
GTP + oxaloacetate
?
-
enzyme mainly functions in gluconeogenesis
-
-
?
GTP + oxaloacetate
?
-
first commited step of gluconeogenesis
-
-
?
GTP + oxaloacetate
?
-
induced by a combination of dibutyryl cAMP, theophylline, and dexamethasone
-
-
?
GTP + oxaloacetate
?
-
first commited step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
role of His-225 and Asp-263 in phosphoenolpyruvate binding
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
decarboxylation of oxaloacetate is the physiological important reaction
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
Cys-306 is important in nucleotide binding and may interact with the 2-OH group in the ribose ring. GTP binds to enzyme tighter than GDP
GDP is a slightly more favorable substrate than IDP in the reverse reaction
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
pace-setting enzyme in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
reaction with GTP is not reported
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
specific for GTP
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
GTP-specific
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
key enzyme involved in the regulation of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
key rate-limiting step in the gluconeogenic pathway, plays a role in the production of glutamine and lysine through the TCA cycle intermediates
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
metal-nucleotide complex serves as substrate, active site structure, a conformational change at the active site occurs during catalysis
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
specifically requires GTP or ITP, structural data of GTP binding
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
committed step in gluconeogenesis
-
?
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
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
GTP-dependent
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
GTP-dependent, enzyme and GTP-binding site structure
phosphoenolpyruvate binds as a 1:1 complex with Na+, structure of the phosphoenolpyruvate-binding site
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
catalyzes the rate-limiting step in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
catalyzes the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
key enzyme of gluconeogenesis, involved in lipid homeostasis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
Modiolus demissus
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
first committed step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
?
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
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
physiological direction of reaction
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
interacts also with ATP, EC 4.1.1.49
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
ir
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
first committed step of gluconeogenesis, important enzyme in the interconversion between C3 and C4 metabolites, recycling of an excess of phosphoenolpyruvate produced from pyruvate
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
the enzyme prefers phosphoenolpyruvate formation from oxaloacetate
-
-
r
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
-
r
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
-
r
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
Modiolus demissus
-
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
lower activity compared to GDP
-
-
?
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
GDP is a slightly more favorable substrate than IDP in the reverse reaction
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
lower activity with IDP than with GDP in the reverse reaction
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
specifically requires GTP or ITP
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
specifically requires GTP or ITP
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
rate limiting enzyme of gluconeogenesis
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
ITP and IDP act as alternative nucleotide cofactors with similar Vmax values and slightly higher Km values
-
-
r
UDP + phosphoenolpyruvate + CO2
UTP + oxaloacetate
-
very low activity
-
?
UDP + phosphoenolpyruvate + CO2
UTP + oxaloacetate
-
very low activity
-
?
additional information
?
-
-
not: adenosine nucleotides
-
?
additional information
?
-
-
reverse reaction: not ADP
-
?
additional information
?
-
-
CO2-oxaloacetate exchange
-
-
?
additional information
?
-
-
catalyzes bicarbonate-dependent phosphorylation of hydroxylamine
-
-
?
additional information
?
-
-
enzyme catalyzes the phosphorylation of glycolate, thioglycolate, and DL-beta-chloroacetate
-
-
?
additional information
?
-
-
not: ATP
-
?
additional information
?
-
-
catalyzes an exchange reaction between HCO3- and the beta-carboxyl group of oxaloacetate
-
-
?
additional information
?
-
-
ADP is completely inactive in carboxylation of oxaloacetate
-
-
?
additional information
?
-
-
ADP is completely inactive in carboxylation of oxaloacetate
-
-
?
additional information
?
-
ADP is a very poor substrate in the reverse reaction
-
?
additional information
?
-
ADP is a very poor substrate in the reverse reaction
-
?
additional information
?
-
-
Mn2+-dependent CO2-oxaloacetate exchange in absence of added nucleotide
-
-
?
additional information
?
-
-
no enzyme activity observed when ADP or CDP is used
-
-
?
additional information
?
-
-
catalyzes bicarbonate-dependent phosphorylation of hydroxylamine
-
-
?
additional information
?
-
-
enzyme catalyzes the phosphorylation of glycolate, thioglycolate, and DL-beta-chloroacetate
-
-
?
additional information
?
-
-
PCK shows no phosphoenolpyruvate-carboxylating activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Ba2+
-
sligthly activates
Ca2+
-
poor activating cation
Co3+
-
study of Co3+-PEPCK with Co3+ bound to enzyme at site n1
Cr3+
-
study of Co3+-PEPCK with Cr3+ bound to enzyme at site n1
Co2+
-
activates
Co2+
-
maximal activity at 4 mM
Co2+
-
significantly activates
Co2+
can substitute Mn2+ but with less efficiency
Co2+
Modiolus demissus
-
Mn2+ or Co2+ required
Co2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Co2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Co2+
21% of the activity with Mn2+
Co2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Co2+: 0.752 mM. When Mg2+ is added as a second cation, in presemce of Mg2+, the Km values for CO2+ in both directions of the reaction are markedly decreased
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
Mg2+
-
no activation
Mg2+
-
sequence contains a putative Mg2+ binding domain
Mg2+
-
absolute requirement of a metal ion, activity is maximal in the presence of both Mn2+ and Mg2+, for single ion activation Mn2+ can be substituted by Mg2+ with a reduced enzyme activity
Mg2+
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mg2+
binding of GTP is Mn2+/Mg2+ dependent
Mg2+
-
maximal activity at 1 mM
Mg2+
can substitute Mn2+ but with less efficiency
Mg2+
-
active site-bound, mode of binding
Mg2+
-
can replace Mn2+ in activation of oxaloacetate decarboxylation
Mg2+
requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+
Mg2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mg2+
-
binds to enzyme more weakly than Mn2+
Mg2+
4.5% of the activity with Mn2+
Mg2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Mg2+: 5.36 mM. When Mg2+ is added as a second cation, the Km values for Mn2+ in both directions of the reaction are markedly decreased to 0.021-0.022 mM
Mn2+
-
enzyme-bound, role of His-225 and Asp-263 in Mn2+ binding, Asp-262 and Thr-249 are also part of the metal binding sites
Mn2+
-
binds directly to the enzyme and binds to the nucleotide resulting in the metal-nucleotide complex
Mn2+
-
enzyme binds Mn2+ at the catalytic site, binary PEPCK-Mn2+ complex, activator Mn2+ enhances the nucleotide binding
Mn2+
-
absolute requirement in oxaloacetate formation
Mn2+
-
absolute requirement of a metal ion, activity is maximal in the presence of both Mn2+ and Mg2+, for single ion activation Mn2+ can be substituted by Mg2+ with a reduced enzyme activity
Mn2+
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mn2+
binding of GTP is Mn2+/Mg2+ dependent
Mn2+
-
maximal activity at 1 mM
Mn2+
most effective activator
Mn2+
-
best activator, enzyme requires two divalent cations, one activates through a direct interaction with enzyme at site n1, located at Asp-295 and Asp-296, the second cation, at site n2, acts in the cation-nucleotide complex that serves as a substrate, role and binding mode of Mn2+, may be a regulator for enzyme in vivo
Mn2+
-
binds to the active site, activates
Mn2+
-
active site-bound, mode of binding
Mn2+
the IC50 values for Mn2+ are 0.009 mM for Mg2+ concentration 2 mM, wild-type, Vmax = 31 micromol/min/mg, 0.607 mM for Mg2+ concentration 2 mM, Y235F mutant, Vmax = 4 micromol/min/mg, 0.073 mM for Mg2+ concentration 2 mM, Y235A mutant, Vmax = 19 micromol/min/mg, 0.058 mM for Mg2+ concentration 2 mM, Y235S mutant, Vmax = 13 micromol/min/mg, 0.0008 mM for wild-type, Vmax = 29 micromol/min/mg, 0.0007 mM for Y235F mutant, Vmax = 31 micromol/min/mg, 0.0004 mM for Y235A mutant, Vmax = 2 micromol/min/mg, 0.0007 mM for Y235S mutant, Vmax = 2 micromol/min/mg, 0.009 mM for wild-type, Mg2+ concentration 5 mM, Vmax = 31 micromol/min/mg, 0.562 mM for Y235F mutant, Mg2+ concentration 5 mM, Vmax = 4 micromol/min/mg, 0.064 mM for Y235A mutant, Mg2+ concentration 5 mM, Vmax = 18 micromol/min/mg, 0.048 mM for Y235S mutant, Mg2+ concentration 5 mM, Vmax = 13 micromol/min/mg, 0.009 mM for wild-type, Mg2+ concentration 7.5 mM, Vmax = 31 micromol/min/mg, 0.521 mM for Y235F mutant, Mg2+ concentration 7.5 mM, Vmax = 4 micromol/min/mg, 0.057 mM for Y235A mutant, Mg2+ concentration 7.5 mM, Vmax = 18 micromol/min/mg, 0.043 mM for Y235S mutant, Mg2+ concentration 7.5 mM, Vmax = 13 micromol/min/mg
Mn2+
-
absolutely required for phosphoenolpyruvate carboxylation
Mn2+
-
half-maximal activation: of phosphoenolpyruvate carboxylation at 2 mM, of oxaloacetate decarboxylation at 0.4 mM, of exchange reaction at 8 mM
Mn2+
Modiolus demissus
-
Km: 0.28 mM
Mn2+
Modiolus demissus
-
Mn2+ or Co2+ required
Mn2+
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Mn2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mn2+
-
required, 4 mM used in assay conditions
Mn2+
-
binds to the active site, activates
Mn2+
-
Mn2+ is the preferred divalent of mitochondrial PEPCK
Mn2+
divalent cation required for reaction, highest activity with Mn2+
Mn2+
in the presence of one divalent cation alone, Mn2+ gives the highest activity. Km for Mn2+: 0.263 mM. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+
Zn2+
Modiolus demissus
-
activates at low levels, inhibits above 0.3 mM
Zn2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
additional information
-
no requirement for a monovalent cation
additional information
not activated by Ca2+, Zn2+, Cu2+ or Ni2+
additional information
no activity with Ca2+, Zn2+, Cu2+, Ni2+, and Sr2+
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0.03
(Z)-3-fluorophosphoenolpyruvate
-
-
0.053 - 0.19
2'-deoxyguanosine 5'-diphosphate
0.71 - 1.05
2'-deoxyguanosine 5'-triphosphate
0.0185 - 9.6
phosphoenolpyruvate
additional information
additional information
-
0.053
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25°C, wild-type enzyme
0.12
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25°C, C306S mutant
0.19
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25°C, C306A mutant
0.71
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25°C, C306A mutant
1.02
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25°C, C306S mutant
1.05
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25°C, wild-type enzyme
0.0133
CO2
-
mitochondrial enzyme
0.0133
CO2
-
CO2 in form of HCO3-
0.0175
CO2
-
cytosolic enzyme
0.0175
CO2
-
CO2 in form of HCO3-
0.066
CO2
-
CO2 in form of HCO3-
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
2.4
CO2
-
pH 7, in presence of 2.3 mM Mn2+
2.4
CO2
-
CO2 in form of HCO3-
4.5
CO2
-
enzyme from autotrophically grown cells
4.5
CO2
-
CO2 in form of KHCO3
4.76
CO2
-
in Tris-HCl (50 mM, pH 7.4), temperature not specified in the publication
6.7
CO2
-
with IDP as cosubstrate, Mn2+ does not affect the Km
6.7
CO2
-
CO2 in form of HCO3-
6.8
CO2
Mg2+ concentration 2 mM, Y235A mutant. Vmax = 21 micromol/min/mg
6.8
CO2
CO2 in form of HCO3-
7
CO2
-
enzyme from heterotrophically grown cells
7
CO2
-
CO2 in form of HCO3-
7.1
CO2
-
with GDP as cosubstrate, Mn2+ does not affect the Km
7.1
CO2
-
CO2 in form of HCO3-
7.2
CO2
Mg2+ concentration 2 mM, Y235F mutant. Vmax = 5 micromol/min/mg
7.2
CO2
CO2 in form of HCO3-
7.5
CO2
Mg2+ concentration 2 mM, Y235S mutant. Vmax = 11 micromol/min/mg
7.5
CO2
CO2 in form of HCO3-
8
CO2
-
CO2 in form of HCO3-
8.3
CO2
pH 7.2, 37°C, bicarbonate
12
CO2
-
CO2 in form of HCO3-
13
CO2
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
13
CO2
Modiolus demissus
-
CO2 in form of HCO3-
15.7
CO2
-
in presence of 0.002 mM Mn2+
15.7
CO2
-
CO2 in form of HCO3-
17
CO2
-
in presence of 0.0035 mM Mn2+
17
CO2
-
CO2 in form of HCO3-
19
CO2
-
CO2 in form of HCO3-
20.7
CO2
Mg2+ concentration 2 mM, wild-type. Vmax = 44 micromol/min/mg
20.7
CO2
CO2 in form of HCO3-
20.9
CO2
-
in presence of 0.02 mM Mn2+
20.9
CO2
-
CO2 in form of HCO3-
31
CO2
-
exchange reaction
31
CO2
-
CO2 in form of HCO3-
46
CO2
-
CO2 in form of HCO3-
0.003
GDP
-
-
0.0119
GDP
-
mitochondrial enzyme
0.02
GDP
-
enzyme form S1 and M2 from embryo, enzyme forms M and S from adult
0.0206
GDP
-
cytosolic enzyme
0.022
GDP
-
enzyme form S2 from embryo
0.023
GDP
-
enzyme form M1 from embryo
0.023
GDP
-
pH 7.4, 25°C, wild-type enzyme
0.024
GDP
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.02516
GDP
-
in Tris-HCl (50 mM, pH 7.4), temperature not specified in the publication
0.03
GDP
-
enzyme form S2 from young chicken
0.031
GDP
-
in presence of 0.0015 mM Mn2+
0.033
GDP
-
enzyme form M1 and S1 from young chicken
0.034
GDP
-
in presence of 0.02 mM Mn2+
0.034
GDP
Mg2+ concentration 2 mM, Y235A mutant. Vmax = 15 micromol/min/mg
0.034
GDP
Mg2+ concentration 7.5 mM, Y235A mutant. Vmax = 15 micromol/min/mg
0.035
GDP
-
in presence of 0.0015 mM Mn2+
0.035
GDP
-
enzyme form M2 from young chicken
0.035
GDP
Mg2+ concentration 5 mM, Y235A mutant. Vmax = 15 micromol/min/mg
0.037
GDP
-
in presence of 0.002 mM Mn2+
0.039
GDP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.04
GDP
Mg2+ concentration 5 mM, Y235S mutant. Vmax = 10 micromol/min/mg
0.041
GDP
Mg2+ concentration 7.5 mM, wild-type. Vmax = 35 micromol/min/mg
0.042
GDP
-
GDP in form of MnGDP-
0.044
GDP
Mg2+ concentration 2 mM, Y235S mutant. Vmax = 11 micromol/min/mg
0.044
GDP
Mg2+ concentration 5 mM, wild-type. Vmax = 35 micromol/min/mg
0.045
GDP
Mg2+ concentration 2 mM, wild-type. Vmax = 33 micromol/min/mg
0.047
GDP
Mg2+ concentration 2 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.053
GDP
Mg2+ concentration 7.5 mM, Y235S mutant. Vmax = 11 micromol/min/mg
0.056
GDP
-
enzyme from autotrophically grown cells
0.06
GDP
Mg2+ concentration 5 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.067
GDP
Mg2+ concentration 7.5 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.07
GDP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.12
GDP
-
enzyme from heterotrophically grown cells
0.12
GDP
-
pH 7.4, 25°C, C306S mutant
0.15
GDP
-
pH 7.4, 25°C, C306A mutant
0.8
GDP
-
at pH 6.3 or at pH 7.2
20.6
GDP
-
in 100 mM HEPES-NaOH, pH 8, 3.6 mM L-malate, 10 mM dithiothreitol, 2 mM MgCl2, 0.2 mM MnCl2, at 37°C
0.0074
GTP
-
mitochondrial enzyme
0.0164
GTP
-
cytosolic enzyme
0.02
GTP
-
enzyme form M2 from embryo, enzyme form S from adult
0.021
GTP
-
enzyme form S1 and S2 from embryo
0.022
GTP
-
enzyme form M1 from embryo and enzyme form M from adult chicken
0.023
GTP
-
in 100 mM HEPES-NaOH, pH 7.2, 100 mM KHCO3, 10 mM dithiothreitol, 2 mM MgCl2, 0.2 mM MnCl2, at 37°C
0.026
GTP
Y235F mutant, Vmax = 41 micromol/min/mg
0.033
GTP
-
enzyme form M1, M2, S2 and S2 from young chicken
0.043
GTP
Y235S mutant, Vmax = 3 micromol/min/mg
0.047
GTP
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.052
GTP
-
pH 7.4, 25°C, wild-type enzyme
0.055
GTP
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.059
GTP
Y235A mutant, Vmax = 3 micromol/min/mg
0.064
GTP
wild-type, Vmax = 39 micromol/min/mg
0.065
GTP
-
enzyme from autotrophically grown cells
0.067
GTP
-
exchange reaction
0.068
GTP
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.13
GTP
-
pH 7.4, 25°C, C306S and C306A mutant
0.141
GTP
-
enzyme from heterotrophically grown cells
0.013
IDP
-
-
0.045
IDP
-
pH 7, in presence of 2.3 mM Mn2+
0.046
IDP
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.1273
IDP
-
in Tris-HCl (50 mM, pH 7.4), temperature not specified in the publication
0.197
IDP
-
IDP in form of MnIDP-
0.3
IDP
-
pH 7.4, 25°C, wild-type enzyme
1.2
IDP
-
pH 7.4, 25°C, C306A mutant
1.38
IDP
-
pH 7.4, 25°C, C306S mutant
0.05
ITP
-
-
0.1
ITP
-
pH 7.4, 25°C, wild-type enzyme
0.11
ITP
-
pH 7.4, 25°C, C306A mutant
0.16
ITP
-
pH 7.4, 25°C, C306S mutant
0.2
ITP
-
exchange reaction
40
ITP
-
ITP in form of MnITP2-
0.004
oxaloacetate
-
pH 7.2
0.004
oxaloacetate
-
in 100 mM HEPES-NaOH, pH 7.2, 100 mM KHCO3, 10 mM dithiothreitol, 2 mM MgCl2, 0.2 mM MnCl2, at 37°C
0.0067
oxaloacetate
wild type enzyme
0.011
oxaloacetate
-
cytosolic enzyme
0.0115
oxaloacetate
mutant enzyme E83A
0.012
oxaloacetate
pH 7.2, 37°C
0.0138
oxaloacetate
mutant enzyme D75N
0.016
oxaloacetate
-
enzyme from autotrophically grown cells
0.0179
oxaloacetate
-
mitochondrial enzyme
0.018
oxaloacetate
60°C, pH 7.0
0.018
oxaloacetate
mutant enzyme D75Q
0.0181
oxaloacetate
pH 7.0, 60°C
0.0183
oxaloacetate
mutant enzyme D75A
0.0189
oxaloacetate
mutant enzyme D75S
0.022
oxaloacetate
-
enzyme from heterotrophically grown cells
0.024
oxaloacetate
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.033
oxaloacetate
wild-type, Vmax = 35 micromol/min/mg
0.038
oxaloacetate
Y235F mutant, Vmax = 39 micromol/min/mg
0.047
oxaloacetate
Y235A mutant, Vmax = 3 micromol/min/mg
0.052
oxaloacetate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.061
oxaloacetate
Y235S mutant, Vmax = 3 micromol/min/mg
0.083
oxaloacetate
-
enzyme form M1 from embryo and enzyme form S2 from young chicken
0.095
oxaloacetate
-
enzyme form M2 and S1 from embryo, enzyme form K1 from young chicken
0.098
oxaloacetate
-
enzyme form M2 from young chicken
0.103
oxaloacetate
-
enzyme form M from adult chicken
0.111
oxaloacetate
-
25°C, apoenzyme
0.113
oxaloacetate
-
enzyme form S1 from young chicken
0.12
oxaloacetate
-
pH 7.4, 25°C, wild-type enzyme
0.123
oxaloacetate
-
25°C, Co3+(n1)-PEPCK
0.125
oxaloacetate
-
enzyme form S from adult chicken
0.131
oxaloacetate
-
25°C, Co3+(n1)-PEPCK-Co3+(n2)-GTP
0.19
oxaloacetate
-
pH 7.4, 25°C, C306S mutant
0.2
oxaloacetate
-
pH 7.4, 25°C, C306A mutant
0.28
oxaloacetate
-
pH 7.5, 30°C, D262N mutant
0.42
oxaloacetate
-
pH 7.5, 30°C, wild-type enzyme
0.749
oxaloacetate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
1
oxaloacetate
-
exchange reaction
1.3
oxaloacetate
-
pH 7.5, 30°C, T249N mutant
2.5
oxaloacetate
-
pH 7.5, 30°C, above, D263N and H225Q mutants
0.0185
phosphoenolpyruvate
-
mitochondrial enzyme
0.02412
phosphoenolpyruvate
-
with IDP as cosubstrate, in Tris-HCl (50 mM, pH 7.4), temperature not specified in the publication
0.0256
phosphoenolpyruvate
-
cytosolic enzyme
0.036
phosphoenolpyruvate
Mn2+ concentration 1.5 mM, Mg2+ concentration 2 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.04252
phosphoenolpyruvate
-
with GDP as cosubstrate, in Tris-HCl (50 mM, pH 7.4), temperature not specified in the publication
0.048
phosphoenolpyruvate
-
-
0.049
phosphoenolpyruvate
-
enzyme form M2 from embryo
0.05
phosphoenolpyruvate
-
enzyme form S1 from embryo
0.051
phosphoenolpyruvate
-
enzyme form M1 from young chicken and enzyme form M from adult chicken
0.053
phosphoenolpyruvate
-
enzyme form M1 and S2 from embryo and enzyme form M2, S1 and S2 from young chicken
0.054
phosphoenolpyruvate
-
enzyme form S from adult chicken
0.063
phosphoenolpyruvate
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.067
phosphoenolpyruvate
-
-
0.1
phosphoenolpyruvate
pH 7.2, 37°C
0.12
phosphoenolpyruvate
-
-
0.13
phosphoenolpyruvate
-
-
0.131
phosphoenolpyruvate
pH 7.0, 60°C
0.131
phosphoenolpyruvate
60°C, pH 7.0
0.217
phosphoenolpyruvate
Mn2+ concentration 1.5 mM, Mg2+ concentration 2 mM, wild-type. Vmax = 31 micromol/min/mg
0.294
phosphoenolpyruvate
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25°C
0.396
phosphoenolpyruvate
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.41
phosphoenolpyruvate
-
pH 6.8
0.41
phosphoenolpyruvate
-
pH 7.4, 25°C, C306S mutant
0.45
phosphoenolpyruvate
-
in 100 mM HEPES-NaOH, pH 8, 3.6 mM L-malate, 10 mM dithiothreitol, 2 mM MgCl2, 0.2 mM MnCl2, at 37°C
0.48
phosphoenolpyruvate
-
pH 7.4, 25°C, C306A mutant
0.55
phosphoenolpyruvate
-
pH 7, in presence of 2.3 mM Mn2+
0.7
phosphoenolpyruvate
-
-
0.8
phosphoenolpyruvate
-
pH 7.2
0.8
phosphoenolpyruvate
-
enzyme from autotrophically grown cells
0.91
phosphoenolpyruvate
-
in presence of 0.0035 mM Mn2+
0.919
phosphoenolpyruvate
Mn2+ concentration 1.5 mM, Mg2+ concentration 2 mM, Y235A mutant. Vmax = 20 micromol/min/mg
0.92
phosphoenolpyruvate
-
in presence of 0.002 mM Mn2+
0.95
phosphoenolpyruvate
-
enzyme from heterotrophically grown cells
0.96
phosphoenolpyruvate
-
in presence of 0.02 mM Mn2+
1.256
phosphoenolpyruvate
Mn2+ concentration 1.5 mM, Mg2+ concentration 2 mM, Y235S mutant. Vmax = 15 micromol/min/mg
1.33
phosphoenolpyruvate
-
in presence of 0.0013 mM Mn2+
2.42
phosphoenolpyruvate
-
pH 7.4, 25°C, wild-type enzyme
9.6
phosphoenolpyruvate
-
pH 6.3
additional information
additional information
-
kinetic data
-
additional information
additional information
-
Km-values for glycolate, thioglycolate and DL-beta-chlorolactate in phosphorylation reaction
-
additional information
additional information
-
Km-values for exchange-reaction
-
additional information
additional information
-
kinetic data for Mn2+ binding
-
additional information
additional information
-
Km for NaHCO3: 5.48 mM
-
additional information
additional information
Km-values for several divalent cations, the presence of 2 mM Mg2+ greatly lowers the Km-values for Mn2+, 144fold in the presence of dithiothreitol and 9.4fold in the absence of dithiothreitol, and for Co2+ by 230fold, influence of divalent cations on the Km-value for phosphoenolpyruvate
-
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Barns, R.J.; Keech, D.B.
Sheep kidney phosphoenolpyruvate carboxylase. Purification and properties
Biochim. Biophys. Acta
276
284-296
1972
Ovis aries
brenda
Jo, J.S.; Ishihara, N.; Kikuchi, G.
Occurence and properties of four forms of phosphoenolpyruvate carboxykinase in the chicken liver
Arch. Biochem. Biophys.
160
246-254
1974
Gallus gallus
brenda
Ting, C.N.; Burgess, D.L.; Chamberlain, J.S.; Keith, T.P.; Falls, K.; Meisler, M.H.
Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20
Genomics
16
698-706
1993
Homo sapiens
brenda
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
brenda
Goto, Y.; Shimizu, J.; Okazaki, T.; Shukuya, R.
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana catesbeiana) liver
J. Biochem.
86
71-78
1979
Lithobates catesbeianus
brenda
Goto, Y.; Shimizu, J.; Shukuya, R.
Purification and molecular characterization of mitochondrial phosphoenolpyruvate carboxykinase from bullfrog (Rana catesbeiana) liver
J. Biochem.
88
1239-1249
1980
Lithobates catesbeianus
brenda
Hebda, C.A.; Nowak, T.
The purification, characterization, and activation of phosphoenolpyruvate carboxykinase from chicken liver mitochondria
J. Biol. Chem.
257
5503-5514
1982
Gallus gallus
brenda
Miyatake, K.; Ito, T.; Kitaoka, S.
Subcellular location and some properties of phosphoenolpyruvate carboxykinase (PEPCK) in Euglena gracilis
Agric. Biol. Chem.
48
2139-2141
1984
Euglena gracilis
-
brenda
Rohrer, S.P.; Saz, H.J.; Nowak, T.
Purification and characteriation of phosphoenolpyruvate carboxykinase from the parasitic helminth Ascaris suum
J. Biol. Chem.
261
13049-13055
1986
Ascaris suum
brenda
Sato, A.; Suzuki, T.; Kochi, H.
Purification and characterization of cytosol-specific phosphoenolpyruvate carboxykinase from chicken liver
J. Biochem.
100
671-678
1986
Gallus gallus
brenda
Gallwitz, W.E.; Jacoby, G.H.; Ray, P.D.; Lambeth, D.O.
Purification and characterization of the isozymes of phosphoenolpyruvate carboxykinase from rabbit liver
Biochim. Biophys. Acta
964
36-45
1988
Oryctolagus cuniculus
brenda
Pnsgen-Schmidt, E.; Schneider, T.; Hammer, U.; Betz, A.
Comparison of phosphoenolpyruvate-carboxykinase from autotrophically and heterotrophically grown Euglena and its role during dark anaerobiosis
Plant Physiol.
86
457-462
1988
Euglena gracilis, Euglena gracilis 1224-5/9
brenda
Bentle, L.A.; Lardy, H.A.
Phosphoenolpyruvate carboxykinase ferroactivator. Purification and some properties
J. Biol. Chem.
252
1431-1440
1977
Rattus norvegicus
brenda
Vial, M.V.; Oelckers, K.B.; Rojas, M.C.; Simpfendrfer, R.W.
Purification, partial kinetic characterization and reactive sulfhydryl groups of the phosphoenolpyruvate carboxykinase from Perumytilus purpuratus adductor muscle
Comp. Biochem. Physiol. B
112
451-460
1995
Perumytilus purpuratus
-
brenda
Williams, C.P.; Postic, C.; Robin, D.; Robin, P.; Parrinello, J.; Shelton, K.; Printz, R.L.; Magnuson, M.A.; Granner, D.K.; Forest, C.; Chalkley, R.
Isolation and characterization of the mouse cytosolic phosphoenolpyruvate carboxykinase (GTP) gene: evidence for tissue-specific hypersensitive sites
Mol. Cell. Endocrinol.
148
67-77
1999
Mus musculus
brenda
Guidinger, P.F.; Nowak, T.
Analogs of oxalacetate as potential substrates for phosphoenolpyruvate carboxykinase
Arch. Biochem. Biophys.
178
131-141
1990
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Bos taurus
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Homo sapiens
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Gallus gallus (P21642)
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Rattus norvegicus (P07379)
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Mycobacterium tuberculosis
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Functional evaluation of serine 252 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
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Saccharomyces cerevisiae (P10963)
brenda
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Homo sapiens (P35558)
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Homo sapiens
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brenda
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Rattus norvegicus
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Hepatic protein kinase B (Akt)-target of rapamycin (TOR)-signalling pathways and intermediary metabolism in rainbow trout (Oncorhynchus mykiss) are not significantly affected by feeding plant-based diets
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Oncorhynchus mykiss (Q98T97)
brenda
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
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Rattus norvegicus
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Stark, R.; Pasquel, F.; Turcu, A.; Pongratz, R.L.; Roden, M.; Cline, G.W.; Shulman, G.I.; Kibbey, R.G.
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Rattus norvegicus
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Activation of SIRT1 by resveratrol represses transcription of the gene for the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) by deacetylating hepatic nuclear factor 4alpha
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Homo sapiens, Mus musculus, Rattus norvegicus
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Biochemistry
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2010
Rattus norvegicus (P07379)
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Asanuma, N.; Kanada, K.; Arai, Y.; Yoshizawa, K.; Ichikawa, T.; Hino, T.
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Streptococcus equinus
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Zhou, J.; Olson, D.G.; Argyros, D.A.; Deng, Y.; van Gulik, W.M.; van Dijken, J.P.; Lynd, L.R.
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Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1313
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Stark, R.; Kibbey, R.G.
The mitochondrial isoform of phosphoenolpyruvate carboxykinase (PEPCK-M) and glucose homeostasis: has it been overlooked?
Biochim. Biophys. Acta
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Gallus gallus
brenda
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
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Rattus norvegicus
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Das, B.; Tandon, V.; Saxena, J.K.; Joshi, S.; Singh, A.R.
Purification and characterization of phosphoenolpyruvate carboxykinase from Raillietina echinobothrida, a cestode parasite of the domestic fowl
Parasitology
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2013
Raillietina echinobothrida
brenda
Oda, H.; Okuda, Y.; Yoshida, Y.; Kimura, N.; Kakinuma, A.
Phenobarbital reduces blood glucose and gluconeogenesis through down-regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression in rats
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Rattus norvegicus
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Lv, Z.; Qiu, L.; Wang, W.; Liu, Z.; Xue, Z.; Yu, Z.; Song, X.; Chen, H.; Wang, L.; Song, L.
A GTP-dependent phosphoenolpyruvate carboxykinase from Crassostrea gigas involved in immune recognition
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Crassostrea gigas (K1QEA6)
brenda
Valle, A.; Cabrera, G.; Cantero, D.; Bolivar, J.
Heterologous expression of the human phosphoenol pyruvate carboxykinase (hPEPCK-M) improves hydrogen and ethanol synthesis in the Escherichia coli dcuD mutant when grown in a glycerol-based medium
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Homo sapiens (Q16822), Homo sapiens
brenda
Hidalgo, J.; Latorre, P.; Carrodeguas, J.A.; Velazquez-Campoy, A.; Sancho, J.; Lopez-Buesa, P.
Inhibition of pig phosphoenolpyruvate carboxykinase isoenzymes by 3-mercaptopicolinic acid and novel inhibitors
PLoS ONE
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2016
Sus scrofa
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