Information on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP)

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

EC NUMBER
COMMENTARY
4.1.1.32
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxykinase (GTP)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
show the reaction diagram
two-step mechanism: phosphorylation followed by decarboxylation, transition state with carbocationic character
-
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
show the reaction diagram
the enzyme decarboxylates oxaloacetate to form the enolate of pyruvate which is then phosphorylated by MgGTP2- on the enzyme
-
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
decarboxylation
-
-
decarboxylation
Q7XAU8
-
PATHWAY
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, cytosol)
-
Biosynthesis of secondary metabolites
-
Citrate cycle (TCA cycle)
-
gluconeogenesis III
-
Glycolysis / Gluconeogenesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
GTP:oxaloacetate carboxy-lyase (adding GTP; phosphoenolpyruvate-forming)
ITP can act as phosphate donor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C4 phosphoenolpyruvate carboxykinase
-
-
C4 phosphoenolpyruvate carboxykinase
Q7XAU8
-
C4 phosphoenolpyruvate carboxykinase
-
-
carboxykinase, phosphopyruvate (guanosine triphosphate)
-
-
-
-
GTP-PEPCK
-
-
GTP/ITP: oxaloacetate carboxylase (transphosphorylating)
-
-
GTP/ITP:oxaloacetate carboxylyase (transphosphorylating)
Q9AGJ6
-
GTP/ITP:oxaloacetate carboxylyase (transphosphorylating)
Mycobacterium smegmatis MC2 155
Q9AGJ6
-
-
GTP/ITP:oxaloacetatecarboxylase (transphosphorylating)
-
-
GTP:oxaloacetate carboxy-lyase
P10963
transphosphorylating, interacts also with ATP, EC 4.1.1.49
oxaloacetate kinase (decarboxylating, GDP)
-
-
-
-
P-enolpyruvate carboxykinase
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxykinase
P35558
-
PEP carboxykinase
-
-
PEP carboxykinase
P10963
-
PEP carboxylase
-
-
-
-
PEP-carboxykinase
Q9AEM1
-
PEPC
Q98T97
-
PEPCK
-
-
-
-
PEPCK
-, Q0KHB7
-
PEPCK
-
-
PEPCK
-
-
PEPCK
P35558
-
PEPCK
P07379
-
PEPCK
Q97VS5
-
-
PEPCK-C
-
-
PEPCK-C
-
cytosolic form
PEPCK-C
P35558
-
PEPCK-C
-
cytosolic form
PEPCK-M
-
-
phosphoenolpyruvate carboxykinase
-
-
-
-
phosphoenolpyruvate carboxykinase
Q9AEM1
-
phosphoenolpyruvate carboxykinase
Q0KHB7
-
phosphoenolpyruvate carboxykinase
-
-
phosphoenolpyruvate carboxykinase
P35558
-
phosphoenolpyruvate carboxykinase
-
-
phosphoenolpyruvate carboxykinase
Q98T97
-
phosphoenolpyruvate carboxykinase
-
-
phosphoenolpyruvate carboxykinase
P10963
-
phosphoenolpyruvate carboxykinase
Q97VS5
-
phosphoenolpyruvate carboxykinase
Q97VS5
-
-
phosphoenolpyruvate carboxykinase (GTP)
-
-
phosphoenolpyruvate carboxykinase, GTP-dependent
-
-
phosphoenolpyruvate carboxykinase, GTP-dependent
-
-
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)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-08-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Holstein cows, dairy cows
-
-
Manually annotated by BRENDA team
strain 1224-5/9
-
-
Manually annotated by BRENDA team
Euglena gracilis 1224-5/9
strain 1224-5/9
-
-
Manually annotated by BRENDA team
nondiabetic nonmenopausal women, aged 19 to 54 years
-
-
Manually annotated by BRENDA team
women, aged 45.7 +/- 4.4 years and have body mass index of 30.3 +/- 1.4 kg m-2
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Modiolus demissus
-
-
-
Manually annotated by BRENDA team
strain MC2 155
SwissProt
Manually annotated by BRENDA team
Mycobacterium smegmatis MC2 155
strain MC2 155
SwissProt
Manually annotated by BRENDA team
three groups of animals examined: high energy diet, high energy diet and exercising, and low energy diet, highest activity in the high energy fed group
-
-
Manually annotated by BRENDA team
male Wistar albino rats
-
-
Manually annotated by BRENDA team
male Wistar rats, enzyme activity is stimulated by intravenous doses of methylprednisolone
-
-
Manually annotated by BRENDA team
six-week-old male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
; strain KOD1, hyperthermophilic archaeon, highest enzyme level when grown with pyruvate as substrate
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q6F494
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
physiological function
-
the enzyme is involved in the initiation of growth, including the induction of amino acid synthesis and energy metabolism
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyguanosine 5'-triphosphate + oxaloacetate
2'-deoxyguanosine 5'-diphosphate + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
Q6F494
poor substrate, poor activity
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
-
the enzyme can also use ATP instead of GTP for oxaloacetate decarboxylation
-
-
ir
dGTP + oxaloacetate
dGDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GDP + (Z)-3-fluorophosphoenolpyruvate + CO2
?
show the reaction diagram
-
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
Modiolus demissus
-
-
-
-
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
P35558
-
-
-
?
GDP + phosphoenolpyruvate + CO2
GTP + oxaloacetate
show the reaction diagram
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
P21642
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
P07379
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-, Q9AGJ6
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
ir
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Modiolus demissus
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-, Q0KHB7
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
-
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q97VS5
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q98T97
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
reaction with GTP is not reported
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AEM1
specific for GTP
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
GTP-dependent
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
Q9AGJ6
GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
GTP-specific
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
role of His-225 and Asp-263 in phosphoenolpyruvate binding
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
specifically requires GTP or ITP, structural data of GTP binding
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AGJ6
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
show the reaction diagram
-
catalyzes the rate-limiting step in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
catalyzes the rate-limiting step in gluconeogenesis, PEPCK expression and growth arrest may be coordinately regulated
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
committed step in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
decarboxylation of oxaloacetate is the physiological important reaction
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AEM1
key enzyme involved in the regulation of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
pace-setting enzyme in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
primary role is the formation of phosphoenolpyruvate in the first committed step of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
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
show the reaction diagram
-
key enzyme of gluconeogenesis, involved in lipid homeostasis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
P10963
interacts also with ATP, EC 4.1.1.49
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
physiological direction of reaction
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
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, the enzyme prefers phosphoenolpyruvate formation from oxaloacetate
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Euglena gracilis 1224-5/9
-
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Mycobacterium smegmatis MC2 155
Q9AGJ6
GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction, 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
show the reaction diagram
Q97VS5
-
-
-
?
GTP + oxaloacetate
?
show the reaction diagram
-
induced by a combination of dibutyryl cAMP, theophylline, and dexamethasone
-
-
-
GTP + oxaloacetate
?
show the reaction diagram
-
first commited step of gluconeogenesis
-
-
-
GTP + oxaloacetate
?
show the reaction diagram
-
enzyme mainly functions in gluconeogenesis
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
-
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
-
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
-
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
-
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
-
-
-
-
IDP + phosphoenolpyruvate + CO2
ITP + oxaloacetate
show the reaction diagram
Modiolus demissus
-
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AGJ6
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
GDP is a slightly more favorable substrate than IDP in the reverse reaction
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
lower activity with IDP than with GDP in the reverse reaction
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
specifically requires GTP or ITP
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
rate limiting enzyme of gluconeogenesis
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
ITP and IDP act as alternative nucleotide cofactors with similar Vmax values and slightly higher Km values
-
-
r
oxaloacetate + ?
pyruvate + CO2
show the reaction diagram
-
ir
-
-
UDP + phosphoenolpyruvate + CO2
UTP + oxaloacetate
show the reaction diagram
-
very low activity
-
-
UDP + phosphoenolpyruvate + CO2
UTP + oxaloacetate
show the reaction diagram
-
very low activity
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
Mycobacterium smegmatis MC2 155
Q9AGJ6
-
-
r
additional information
?
-
-
catalyzes an exchange reaction between HCO3- and the beta-carboxyl group of oxaloacetate
-
-
-
additional information
?
-
-
CO2-oxaloacetate exchange
-
-
-
additional information
?
-
-
ADP is completely inactive in carboxylation of oxaloacetate
-
-
-
additional information
?
-
-
catalyzes bicarbonate-dependent phosphorylation of hydroxylamine
-
-
-
additional information
?
-
-
enzyme catalyzes the phosphorylation of glycolate, thioglycolate, and DL-beta-chloroacetate
-
-
-
additional information
?
-
-
Mn2+-dependent CO2-oxaloacetate exchange in absence of added nucleotide
-
-
-
additional information
?
-
-
not: ATP
-
?
additional information
?
-
Q9AGJ6
ADP is a very poor substrate in the reverse reaction
-
?
additional information
?
-
-
not: adenosine nucleotides
-
?
additional information
?
-
-
reverse reaction: not ADP
-
?
additional information
?
-
-
PCK shows no phosphoenolpyruvate-carboxylating activity
-
-
-
additional information
?
-
Mycobacterium smegmatis MC2 155
Q9AGJ6
ADP is a very poor substrate in the reverse reaction
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AGJ6
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
show the reaction diagram
-
catalyzes the rate-limiting step in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
catalyzes the rate-limiting step in gluconeogenesis, PEPCK expression and growth arrest may be coordinately regulated
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
committed step in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
decarboxylation of oxaloacetate is the physiological important reaction
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q9AEM1
key enzyme involved in the regulation of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
pace-setting enzyme in gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
primary role is the formation of phosphoenolpyruvate in the first committed step of gluconeogenesis
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first committed step of gluconeogenesis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
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
show the reaction diagram
-
key enzyme of gluconeogenesis, involved in lipid homeostasis
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Q6F494
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
?
show the reaction diagram
-
induced by a combination of dibutyryl cAMP, theophylline, and dexamethasone
-
-
-
GTP + oxaloacetate
?
show the reaction diagram
-
first commited step of gluconeogenesis
-
-
-
GTP + oxaloacetate
?
show the reaction diagram
-
enzyme mainly functions in gluconeogenesis
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
Mycobacterium smegmatis MC2 155
Q9AGJ6
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
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
r
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
rate limiting enzyme of gluconeogenesis
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
IDP
-
stimulates Mn2+-dependent CO2-oxaloacetate exchange
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
sligthly activates
Ca2+
-
poor activating cation
Co2+ 
Q6F494
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
Co2+
-
activates; Km: 0.055 mM
Co2+
-
activates; maximal activity at 4 mM
Co2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Co2+
Modiolus demissus
-
Mn2+ or Co2+ required
Co2+
Q9AGJ6
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Co2+
-
significantly activates
Co2+
Q6F494
21% of the activity with Mn2+
Co2+
P21642
can substitute Mn2+ but with less efficiency
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
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
Fe2+
-
Fe2+ alone does not stimulate, Fe2+ + ferroactivator, stimulate in both directions of the reaction
Mg2+ 
Q6F494
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
Mg2+
-
can replace Mn2+ in activation of oxaloacetate decarboxylation
Mg2+
-
activates; Km: 0.043 mM; maximal activity at 1 mM
Mg2+
-
no activation
Mg2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mg2+
-
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mg2+
-
binds to enzyme more weakly than Mn2+
Mg2+
Q9AGJ6
requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+
Mg2+
-
active site-bound, mode of binding
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+
Q6F494
4.5% of the activity with Mn2+
Mg2+
P21642
can substitute Mn2+ but with less efficiency
Mg2+
-, Q0KHB7
required
Mg2+
-
required
Mn2+ 
Q6F494
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+
Mn2+
-
absolutely required for phosphoenolpyruvate carboxylation; half-maximal activation: of phosphoenolpyruvate carboxylation at 2 mM, of oxaloacetate decarboxylation at 0.4 mM, of exchange reaction at 8 mM
Mn2+
-
absolutely required for phosphoenolpyruvate carboxylation
Mn2+
-
activates
Mn2+
-
activates; Km: 0.045 mM; maximal activity at 1 mM
Mn2+
-
activates; binds directly to the enzyme and binds to the nucleotide resulting in the metal-nucleotide complex; Km: 0.77 mM
Mn2+
-
activates
Mn2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Mn2+
-
absolute requirement in oxaloacetate formation
Mn2+
Modiolus demissus
-
Km: 0.28 mM; Mn2+ or Co2+ required
Mn2+
-
reaction in the presence of divalent cations, Mn2+ and Mg2+
Mn2+
-
enzyme binds Mn2+ at the catalytic site, binary PEPCK-Mn2+ complex, activator Mn2+ enhances the nucleotide binding
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+
-
Mn2+-dependent
Mn2+
Q9AGJ6
requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator
Mn2+
-
active site-bound, mode of binding
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+
-
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+
Q6F494
divalent cation required for reaction, highest activity with Mn2+
Mn2+
P21642
most effective activator
Mn2+
-
required
Mn2+
P35558
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
Zn2+
-
divalent metal ion required, decreasing order of effectiveness: Co2+, Mn2+, Zn2+, Mg2+
Zn2+
Modiolus demissus
-
activates at low levels, inhibits above 0.3 mM
Mn2+
-
Mn2+ is the preferred divalent of mitochondrial PEPCK
additional information
-
no requirement for a monovalent cation
additional information
Q9AGJ6
not activated by Ca2+, Zn2+, Cu2+ or Ni2+
additional information
Q6F494
no activity with Ca2+, Zn2+, Cu2+, Ni2+, and Sr2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(Z)-Phosphoenol-3-bromopyruvate
-
linear competitive
1-allyl-3-butyl-8-methylxanthine
-
weak, competitive inhibitor with respect to GTP, IC50: 0.225 mM in the decarboxylation direction, modifications at N-1 and C-8 improve the inhibitory activity by more than 100fold
2,3-Butanedione
-
-
2-oxobutanoate
-
weak
2-oxoglutarate
-
above 5.0 mM, weak
2-oxoglutarate
-
competitive with respect to both oxaloacetate and phosphoenolpyruvate
2-oxoglutarate
-
-
2-oxoglutarate
-
in both directions, competitive with respect to oxaloacetate or phosphoenolpyruvate, noncompetitive with respect GTP or Mn2+
2-oxoglutarate
Q6F494
weak inhibition
2-Phosphoglycolate
-
-
3-Aminopicolinic acid
Modiolus demissus
-
-
3-Mercaptopicolinic acid
Modiolus demissus
-
strong
3-Mercaptopicolinic acid
-
reversible, non-competitive inhibitor, IC50: in the 0.02 mM range
3-Nitro-2-oxopropionic acid
-
weak
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
inhibits wild-type enzyme, but not C306A or C306S mutant enzymes
8-Azidoguanosine 5'-triphosphate
-
photoinactivation is caused by formation of an intramolecular cystine disulfide bridge
Acetopyruvate
-
weak noncompetitive
ADP
Modiolus demissus
-
uncompetitive with respect to IDP, partially competitive with respect to phosphoenolpyruvate
alpha-(Dihydroxyphosphinylmethyl) acrylic acid
-
weak linear competitive
alpha-ketoglutarate
Q9AGJ6
inhibits oxaloacetate formation, mixed-type inhibition
ATP
-
competitive against GTP
ATP
Modiolus demissus
-
strong
beta-sulfopyruvate
-
-
beta-sulfopyruvate
-
mixed inhibitor of PEPCK against oxaloacetate
citrate
-
above 5.0 mM, weak
Co3+-GDP
-
competitive inhibitor
Co3+-GTP
-
competitive inhibitor
Cr3+-GDP
-
competitive inhibitor
Cr3+-GTP
-
competitive inhibitor
dithiothreitol
-
5 mM, 19% inhibition
DL-3-Nitro-2-hydroxypropionic acid
-
weak
DL-isocitrate
-
above 5.0 mM, weak
EDTA
-
0.5 mM, 86% inhibition
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
glycerate
-
D-glycerate, L-glycerate and DL-glycerate, weak noncompetitive
GMP
-
competitive with GDP
Hydroxymalonate
Modiolus demissus
-
slight
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
-
iodoacetamide
-
guanine nucleotides, IDP and Mn2+ protect
iodoacetamide
-
-
iodoacetate
-
-
ITP
-
competitive against GTP, IDP and phosphoenolpyruvate
KCl
Modiolus demissus
-
120 mM, 50% inhibition
KCl
Q9AGJ6
0.5 M, 50% inhibition
KHCO3
-
above 0.1 M inhibits the oxaloacetate-forming activity
L-alanine
-, Q0KHB7
-
malate
-
above 5.0 mM, weak
malate
-
DL-malate, weak
malonate
-
weak
Mg2+
-
Mg2+ reduces mitochondrial PEPCK activity
MgCl2
-
1.5 mM, 62% inhibition
NaCl
Modiolus demissus
-
115 mM, 50% inhibition
NaCl
Q9AGJ6
0.5 M, 50% inhibition
oxalate
-
above 5.0 mM, weak
oxalate
-
weak, noncompetitive
oxalate
Q9AGJ6
potent inhibitor of oxaloacetate formation, mixed-type inhibition
pyruvate
Q6F494
weak inhibition
Quinolinic acid
-
strongly inhibits the enzyme activated by ferroactivator and Fe2+, no inhibition of Mn2+-activated enzyme
succinate
-
above 5.0 mM, weak
Tartronate
-
weak
Zn2+
Modiolus demissus
-
activates at low levels, inhibits above 0.3 mM
Mn2+
-
Mn2+ concentrations above 0.7 mM inhibit the His-tagged enzyme
additional information
-
vanadate inhibits transcription of the phosphoenolpyruvate carboxykinase gene
-
additional information
-
not inhibited by adenosine nucleotides
-
additional information
-
insulin is a potent dominant repressor of PEPCK gene transcription and causes a rapid decrease of PEPCK mRNA
-
additional information
-
study of several modified 3-alkyl-1,8-dibenzylxanthines as competitive inhibitors with respect to GTP, IC50-values
-
additional information
-
not inhibited by dithiothreitol
-
additional information
-
reduced expression of mRNA when cells are cultured in conditioned medium obtained from LPS-stimulated Kupffer cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Q9AGJ6
maximum stimulation at 75 mM
dithiothreitol
Q9AGJ6
maximum at 10-40 mM, 30% stimulation
Ferroactivator
-
ferroactivator + Fe2+, stimulates both directions of the reaction
-
ITP
-
stimulates Mn2+-dependent CO2-oxaloacetate exchange
reduced glutathione
Q9AGJ6
maximum stimulation at 20 mM
thiol-containing reducing agent
Q9AGJ6
activates
-
Mn2+
-
activity regulator, 0.7 mM leads to full enzyme stimulation
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
P35558
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
-
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
-
PEPCK mRNA expression in the subcutaneous adipose tissues is associated with body mass index and plasma triacylglycerol and total cholesterol levels, but is not correlated with insulin resistance index
-
additional information
-
ketogenic diet-fed rats have increased fat mass and phosphoenolpyruvate carboxykinase activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
(Z)-3-fluorophosphoenolpyruvate
-
-
0.053
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, wild-type enzyme
0.12
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, C306S mutant
0.19
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, C306A mutant
0.71
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, C306A mutant
1.02
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, C306S mutant
1.05
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, wild-type enzyme
2.23
-
ADP
Q6F494
pH 7.0, 60C
0.465
-
ATP
Q6F494
pH 7.0, 60C
0.814
-
CO2
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
1.194
-
CO2
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
8.3
-
CO2
Q9AGJ6
pH 7.2, 37C, bicarbonate
0.003
-
GDP
-
-
0.0075
-
GDP
-
-
0.0119
-
GDP
-
mitochondrial enzyme
0.0185
-
GDP
Q6F494
pH 7.0, 60C
0.019
-
GDP
Q6F494
60C, pH 7.0
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
0.022
-
GDP
-
-
0.023
-
GDP
-
enzyme form M1 from embryo
0.023
-
GDP
-
pH 7.4, 25C, wild-type enzyme
0.024
-
GDP
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
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
P35558
Mg2+ concentration 2 mM, Y235A mutant. Vmax = 15 micromol/min/mg; Mg2+ concentration 7.5 mM, Y235A mutant. Vmax = 15 micromol/min/mg
0.035
-
GDP
-
enzyme form M2 from young chicken
0.035
-
GDP
-
in presence of 0.0015 mM Mn2+
0.035
-
GDP
P35558
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 25C
0.04
-
GDP
P35558
Mg2+ concentration 5 mM, Y235S mutant. Vmax = 10 micromol/min/mg
0.041
-
GDP
P35558
Mg2+ concentration 7.5 mM, wild-type. Vmax = 35 micromol/min/mg
0.044
-
GDP
P35558
Mg2+ concentration 2 mM, Y235S mutant. Vmax = 11 micromol/min/mg; Mg2+ concentration 5 mM, wild-type. Vmax = 35 micromol/min/mg
0.045
-
GDP
P35558
Mg2+ concentration 2 mM, wild-type. Vmax = 33 micromol/min/mg
0.047
-
GDP
P35558
Mg2+ concentration 2 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.053
-
GDP
P35558
Mg2+ concentration 7.5 mM, Y235S mutant. Vmax = 11 micromol/min/mg
0.056
-
GDP
-
enzyme from autotrophically grown cells
0.059
-
GDP
-
-
0.06
-
GDP
P35558
Mg2+ concentration 5 mM, Y235F mutant. Vmax = 3 micromol/min/mg
0.066
-
GDP
Q9AGJ6
pH 7.2, 37C
0.067
-
GDP
P35558
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 25C
0.12
-
GDP
-
enzyme from heterotrophically grown cells
0.12
-
GDP
-
pH 7.4, 25C, C306S mutant
0.15
-
GDP
-
pH 7.4, 25C, 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 37C
0.0074
-
GTP
-
mitochondrial enzyme
0.013
-
GTP
Q9AGJ6
pH 7.2, 37C
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
0.0211
-
GTP
-
-
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 37C
0.026
-
GTP
P35558
Y235F mutant, Vmax = 41 micromol/min/mg
0.033
-
GTP
-
enzyme form M1, M2, S2 and S2 from young chicken
0.036
-
GTP
Q6F494
60C, pH 7.0
0.0361
-
GTP
Q6F494
pH 7.0, 60C
0.043
-
GTP
P35558
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 25C
0.052
-
GTP
-
pH 7.4, 25C, wild-type enzyme
0.055
-
GTP
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.059
-
GTP
P35558
Y235A mutant, Vmax = 3 micromol/min/mg
0.064
-
GTP
P35558
wild-type, Vmax = 39 micromol/min/mg
0.065
-
GTP
-
-
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 25C
0.13
-
GTP
-
pH 7.4, 25C, C306S and C306A mutant
0.141
-
GTP
-
enzyme from heterotrophically grown cells
1.6
-
GTP
-
pH 7.2
0.0133
-
HCO3-
-
mitochondrial enzyme
0.0175
-
HCO3-
-
cytosolic enzyme
0.066
-
HCO3-
-
-
2.4
-
HCO3-
-
pH 7, in presence of 2.3 mM Mn2+
6.7
-
HCO3-
-
with IDP as cosubstrate, Mn2+ does not affect the Km
6.8
-
HCO3-
P35558
Mg2+ concentration 2 mM, Y235A mutant. Vmax = 21 micromol/min/mg
7
-
HCO3-
-
enzyme from heterotrophically grown cells
7.1
-
HCO3-
-
with GDP as cosubstrate, Mn2+ does not affect the Km
7.2
-
HCO3-
P35558
Mg2+ concentration 2 mM, Y235F mutant. Vmax = 5 micromol/min/mg
7.5
-
HCO3-
P35558
Mg2+ concentration 2 mM, Y235S mutant. Vmax = 11 micromol/min/mg
8
-
HCO3-
-
pH 6.3
13
-
HCO3-
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
15.7
-
HCO3-
-
in presence of 0.002 mM Mn2+
17
-
HCO3-
-
in presence of 0.0035 mM Mn2+
19
-
HCO3-
-
-
20.7
-
HCO3-
P35558
Mg2+ concentration 2 mM, wild-type. Vmax = 44 micromol/min/mg
20.9
-
HCO3-
-
in presence of 0.02 mM Mn2+
31
-
HCO3-
-
exchange reaction
46
-
HCO3-
-
pH 7.2
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
0.0712
-
IDP
Q6F494
pH 7.0, 60C
0.0715
-
IDP
-
-
0.182
-
IDP
-
-
0.29
-
IDP
Q9AGJ6
pH 7.2, 37C
0.3
-
IDP
-
pH 7.4, 25C, wild-type enzyme
0.8
-
IDP
-
pH 6.3
1.2
-
IDP
-
pH 7.4, 25C, C306A mutant
1.38
-
IDP
-
pH 7.4, 25C, C306S mutant
2.5
-
IDP
-
pH 7.2
0.05
-
ITP
-
-
0.0715
-
ITP
Q6F494
pH 7.0, 60C
0.1
-
ITP
-
pH 7.4, 25C, wild-type enzyme
0.11
-
ITP
-
pH 7.4, 25C, C306A mutant
0.13
-
ITP
-
-
0.16
-
ITP
-
pH 7.4, 25C, C306S mutant
0.2
-
ITP
-
exchange reaction
0.279
-
ITP
-
-
4
-
ITP
-
pH 7.2
4.5
-
KHCO3
-
enzyme from autotrophically grown cells
0.042
-
MnGDP2-
-
-
-
0.197
-
MnIDP-
-
-
-
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 37C
0.0067
-
oxaloacetate
-, Q9AGJ6
wild type enzyme
0.011
-
oxaloacetate
-
cytosolic enzyme
0.0115
-
oxaloacetate
-, Q9AGJ6
mutant enzyme E83A
0.012
-
oxaloacetate
Q9AGJ6
pH 7.2, 37C
0.0138
-
oxaloacetate
-, Q9AGJ6
mutant enzyme D75N
0.014
-
oxaloacetate
-
-
0.016
-
oxaloacetate
-
enzyme from autotrophically grown cells
0.0179
-
oxaloacetate
-
mitochondrial enzyme
0.018
-
oxaloacetate
Q6F494
60C, pH 7.0
0.018
-
oxaloacetate
-, Q9AGJ6
mutant enzyme D75Q
0.0181
-
oxaloacetate
Q6F494
pH 7.0, 60C
0.0183
-
oxaloacetate
-, Q9AGJ6
mutant enzyme D75A
0.0189
-
oxaloacetate
-, Q9AGJ6
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
0.026
-
oxaloacetate
-
-
0.033
-
oxaloacetate
P35558
wild-type, Vmax = 35 micromol/min/mg
0.038
-
oxaloacetate
P35558
Y235F mutant, Vmax = 39 micromol/min/mg
0.047
-
oxaloacetate
P35558
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 25C
0.061
-
oxaloacetate
P35558
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
-
25C, apoenzyme
0.113
-
oxaloacetate
-
enzyme form S1 from young chicken
0.12
-
oxaloacetate
-
pH 7.4, 25C, wild-type enzyme
0.123
-
oxaloacetate
-
25C, Co3+(n1)-PEPCK
0.125
-
oxaloacetate
-
enzyme form S from adult chicken
0.131
-
oxaloacetate
-
25C, Co3+(n1)-PEPCK-Co3+(n2)-GTP
0.19
-
oxaloacetate
-
pH 7.4, 25C, C306S mutant
0.2
-
oxaloacetate
-
pH 7.4, 25C, C306A mutant
0.28
-
oxaloacetate
-
pH 7.5, 30C, D262N mutant
0.42
-
oxaloacetate
-
pH 7.5, 30C, wild-type enzyme
0.749
-
oxaloacetate
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
1
-
oxaloacetate
-
exchange reaction
1.3
-
oxaloacetate
-
pH 7.5, 30C, T249N mutant
2.5
-
oxaloacetate
-
pH 7.5, 30C, above, D263N and H225Q mutants
0.0185
-
phosphoenolpyruvate
-
mitochondrial enzyme
0.0256
-
phosphoenolpyruvate
-
cytosolic enzyme
0.036
-
phosphoenolpyruvate
P35558
Mn2+ concentration 1.5 mM, Mg2+ concentration 2 mM, Y235F mutant. Vmax = 3 micromol/min/mg
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 25C
0.067
-
phosphoenolpyruvate
-
-
0.1
-
phosphoenolpyruvate
Q9AGJ6
pH 7.2, 37C
0.12
-
phosphoenolpyruvate
-
-
0.13
-
phosphoenolpyruvate
-
-
0.131
-
phosphoenolpyruvate
Q6F494
60C, pH 7.0; pH 7.0, 60C
0.217
-
phosphoenolpyruvate
P35558
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 25C
0.396
-
phosphoenolpyruvate
Modiolus demissus
-
in presence of 1 mM MnCl2 and 1 mM MgCl2
0.41
-
phosphoenolpyruvate
-
pH 7.4, 25C, C306S mutant
0.41
-
phosphoenolpyruvate
-
pH 6.8
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 37C
0.48
-
phosphoenolpyruvate
-
pH 7.4, 25C, 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
P35558
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
P35558
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, 25C, wild-type enzyme
9.6
-
phosphoenolpyruvate
-
pH 6.3
40
-
MnITP2-
-
-
additional information
-
additional information
-
Km-values for exchange-reaction
-
additional information
-
additional information
-
Km-values for glycolate, thioglycolate and DL-beta-chlorolactate in phosphorylation reaction
-
additional information
-
additional information
-
kinetic data for Mn2+ binding
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
Q9AGJ6
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
-
additional information
-
additional information
-
Km for NaHCO3: 5.48 mM
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, C306S mutant
0.5
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, C306A mutant
4.6
-
2'-deoxyguanosine 5'-diphosphate
-
pH 7.4, 25C, wild-type enzyme
2.3
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, C306A mutant
2.4
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, C306S mutant
3.4
-
2'-deoxyguanosine 5'-triphosphate
-
pH 7.4, 25C, wild-type enzyme
1
-
CO2
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
19
-
CO2
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
1
-
GDP
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
3.5
-
GDP
-
pH 7.4, 25C, C306S mutant
4.1
-
GDP
-
pH 7.4, 25C, C306A mutant
6.5
-
GDP
-
pH 7.4, 25C, wild-type enzyme
19
-
GDP
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
10.3
-
GTP
-
pH 7.4, 25C, C306S mutant
12.4
-
GTP
-
pH 7.4, 25C, C306A mutant
13.9
-
GTP
-
pH 7.4, 25C, wild-type enzyme
14
-
GTP
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
54
-
GTP
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
2.3
-
IDP
-
pH 7.4, 25C, C306S mutant
2.4
-
IDP
-
pH 7.4, 25C, C306A mutant
6.9
-
IDP
-
pH 7.4, 25C, wild-type enzyme
10.7
-
ITP
-
pH 7.4, 25C, C306A mutant
12.8
-
ITP
-
pH 7.4, 25C, C306S mutant
13.3
-
oxaloacetate
-
pH 7.4, 25C, C306S mutant
14
-
oxaloacetate
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
14.5
-
oxaloacetate
-
pH 7.4, 25C, C306A mutant
17.8
-
oxaloacetate
-
pH 7.4, 25C, wild-type enzyme
54
-
oxaloacetate
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
1
-
phosphoenolpyruvate
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
1.8
-
phosphoenolpyruvate
-
pH 7.4, 25C, C306A mutant
2.1
-
phosphoenolpyruvate
-
pH 7.4, 25C, C306S mutant
6.1
-
phosphoenolpyruvate
-
pH 6.8
9.3
-
phosphoenolpyruvate
-
pH 7.4, 25C, wild-type enzyme
19
-
phosphoenolpyruvate
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
15.6
-
ITP
-
pH 7.4, 25C, wild-type enzyme
additional information
-
additional information
-
kcat for NaHCO3: 6.7 s-1
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.2
-
CO2
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
8725
16
-
CO2
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
8725
14
-
GDP
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
10807
510
-
GDP
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
10807
270
-
GTP
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
11186
790
-
GTP
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
11186
19
-
oxaloacetate
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
14857
1000
-
oxaloacetate
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
14857
15
-
phosphoenolpyruvate
-
mutant enzyme A467G, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
15572
66
-
phosphoenolpyruvate
-
wild type enzyme, in 50 mM HEPES pH 7.5, 10 mM dithiothreitol, 4 mM MgCl2, at 25C
15572
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
120
-
KCl
Modiolus demissus
-
-
115
-
NaCl
Modiolus demissus
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.225
-
1-allyl-3-butyl-8-methylxanthine
-
weak, competitive inhibitor with respect to GTP, IC50: 0.225 mM in the decarboxylation direction, modifications at N-1 and C-8 improve the inhibitory activity by more than 100fold
0.02
-
3-Mercaptopicolinic acid
-
reversible, non-competitive inhibitor, IC50: in the 0.02 mM range
0.3
-
KHCO3
-
-
9.3
-
L-alanine
-, Q0KHB7
in 100 mM imidazole-HCl buffer (pH 6.6), at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.06
-
-, Q9AGJ6
mutant enzyme D78A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
0.13
-
-, Q9AGJ6
mutant enzyme D78A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
0.15
-
-, Q9AGJ6
mutant enzyme D78A, oxaloacetate-forming activity in the presence of 2 mM Mn2+
0.36
-
-, Q9AGJ6
mutant enzyme E83A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
0.4
-
-, Q9AGJ6
mutant enzyme E83A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
1
-
-, Q9AGJ6
mutant enzyme E83A, oxaloacetate-forming activity in the presence of 2 mM Mn2+
1.81
-
Modiolus demissus
-
-
2.93
-
-
-
4.75
-
-
-
10.6
-
-, Q9AGJ6
mutant enzyme D75A, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
12.3
-
-, Q9AGJ6
wild type enzyme, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2+
13.5
-
-
mitochondrial enzyme
14.5
-
-
cytosolic enzyme
15.5
-
-, Q9AGJ6
mutant enzyme D75A, phosphoenolpyruvate-forming activity in the presence of 0.2 mM Mn2
16.7
-
-
carboxylation of phosphoenolpyruvate
17.7
-
-
-
19.9
-
-
decarboxylation of oxaloacetate
29.4
-
-, Q9AGJ6
wild type enzyme, oxaloacetate-forming activity in the presence of 2 mM Mn2+
43
-
-, Q9AGJ6
wild type enzyme, oxaloacetate-forming activity in the presence of 0.2 mM Mn2+
46.5
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q9AGJ6
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-, Q0KHB7
separation of mitochondrial and cytosolic fraction shows that more than 92% of the PEPCK enzyme activity is cytosolic in gills, digestive gland, mantle and muscle; specific activity: 4.7 U/g (digestive glands), 0.3 U/g (gill), 3.2 U/g (gonads), 0.3 U/g (mantle), 10.9 U/g (muscle)
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
-
-
phosphoenolpyruvate carboxylation and exchange reaction in presence of Mn2+
6.5
-
-
carboxylation, with Mn2+
6.5
-
-
carboxylation
6.6
-
Modiolus demissus
-
-
7
7.4
Q9AGJ6
at 37C
7.4
-
-
assay at
7.5
-
-
carboxylation, with Mg2+
7.5
-
-
oxaloacetate decarboxylation and exchange reaction in presence of Mg2+; oxaloacetate decarboxylation in presence of Mn2+
7.5
-
-
carboxylation, enzyme from autotrophically grown cells
7.5
-
-
assay at
7.6
-
-
carboxylation, enzyme from heterotrophically grown cells
8.5
-
-
decarboxylation
8.8
-
-
decarboxylation, enzyme from autotrophically and heterotrophically grown cells
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
pH 6: about 50% of maximal activity, pH 8: about 25% of maximal activity
6
8
Q6F494
pH 6.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
6.25
9
-
enzyme activity in the pH range of 6.25-9
6.3
7.5
Modiolus demissus
-
about 50% of maximal activity at pH 6.3 and pH 7.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
37
-
-
assay at
70
-
Q9AGJ6
at pH 7.2
additional information
-
-
assay at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
90
Q6F494
50C: about 45% of maximal activity, 90C: about 80% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectric focusing
4.61
-
-
theoretically calculated pI
5.5
-
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
rodent adipocyte
Manually annotated by BRENDA team
-
grown autotrophically with CO2 in the light. The yield is higher when an additional carbon source like glucose is added. Highest yields result if both glucose and CO2 are provided together in the dark. No activity in cells provided with CO2 alone and kept in the dark
Manually annotated by BRENDA team
Euglena gracilis 1224-5/9
-
grown autotrophically with CO2 in the light. The yield is higher when an additional carbon source like glucose is added. Highest yields result if both glucose and CO2 are provided together in the dark. No activity in cells provided with CO2 alone and kept in the dark
-
Manually annotated by BRENDA team
-
cultured cells in co-culture with lipopolysaccharide stimulated Kupffer cells
Manually annotated by BRENDA team
-
Reuber H365 hepatoma cells
Manually annotated by BRENDA team
-
Reuber H365 hepatoma cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
of dairy cows during the transition to lactation
Manually annotated by BRENDA team
-, Q0KHB7
; PEPCK mRNAs and enzyme activities are measured in muscle during prolonged hypoxia for 20 days. The PEPCK mRNA ratio in hypoxic muscle significantly increases at day 10 simultaneously to the PEPCK enzyme activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
2 enzyme forms exist in livers of embryos and young chicken, S1 and S2. 1 enzyme form exists in liver of adults, S
Manually annotated by BRENDA team
Modiolus demissus
-
-
Manually annotated by BRENDA team
-
cytosolic isoform
Manually annotated by BRENDA team
-
cytosolic and mitochondrial isoform of PEPCK, encoded by two different nuclear genes, expression of cytosolic PEPCK mRNA is transiently increased during early lactation
Manually annotated by BRENDA team
-
2 enzyme forms exist in livers of embryos and young chicken, M1 and M2. 1 enzyme form exists in liver of adults, M
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mitochondrial isoform
Manually annotated by BRENDA team
-
cytosolic and mitochondrial isoform of PEPCK, encoded by two different nuclear genes, transition to lactation do not alter the mitochondrial PEPCK expression
Manually annotated by BRENDA team
Q9AGJ6
recombinant enzyme
-
Manually annotated by BRENDA team
-
recombinant enzyme
-
Manually annotated by BRENDA team
Mycobacterium smegmatis MC2 155
-
recombinant enzyme
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6925
-
-, Q0KHB7
deduced from cDNA
24000
-
-
all four enzyme forms, gel filtration
42000
-
-
mitochondrial enzyme, gel filtration
50000
-
-
gel filtration
56000
-
-
mitochondrial enzyme, gel filtration
60000
-
-
cytosolic enzyme, gel filtration
65000
-
-
gel filtration
65000
-
-
cytosolic enzyme, gel filtration
67000
-
-
-
67310
-
P21642
mature protein, calculated from amino acid sequence
67540
-
-
recombinant enzyme, mass spectrometry
68500
-
P35558
-
69250
-
-, Q0KHB7
calculated from amino acid sequence
70000
-
Modiolus demissus
-
gel filtration
71000
-
-
glycerol density gradient centrifugation
71000
-
-
gel filtration
71200
-
-, Q9AGJ6
calculated from the nucleic acid sequence-derived amino acid sequence
72000
-
-
glycerol gradient centrifugation
72000
-
-
SDS-PAGE
74000
-
-
gel filtration
75400
-
-
high speed equilibrium sedimentation
80000
-
-
non-denaturing PAGE
83000
-
-
gel filtration
83200
-
Q9AGJ6
gel filtration
85000
-
-
gel filtration
284000
-
Q6F494
gel filtration
550000
-
-
enzyme from heterotrophically grown cells, gel filtration
761000
-
-
enzyme from autotrophically grown cells, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 69448, recombinant enzyme, mass spectrometry
?
-
x * 62254, calculated from amino acid sequence
dimer
-
2 * 247000, enzyme from heterotrophically grown cells, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
Euglena gracilis 1224-5/9
-
2 * 247000, enzyme from heterotrophically grown cells, SDS-PAGE
-
homotetramer
Q6F494
4 * 70000, SDS-PAGE; 4 * 72039, calculated from sequence
monomer
-
1 * 71000-72000, SDS-PAGE
monomer
-
1 * 71500, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 70500, SDS-PAGE under reducing conditions
monomer
-
1 * 75000-80000, SDS-PAGE
monomer
-
1 * 68000, cytosolic enzyme, SDS-PAGE
monomer
-
1 * 65000, mitochondrial enzyme, SDS-PAGE
monomer
-
1 * 74000, SDS-PAGE
monomer
-
1 * 69500, SDS-PAGE
monomer
Modiolus demissus
-
1 * 70000, SDS-PAGE
monomer
Q9AGJ6
1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry
monomer
-
1 * 67512, calculated from the amino acid sequence
monomer
-
1 * 67000
monomer
Mycobacterium smegmatis MC2 155
-
1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry
-
tetramer
Q6F494
4 * 72036, subunit mass calculated from the deduced amino acid sequence
tetramer
-
four identical monomers per asymmetric unit which pack together as two dimers in the crystal
trimer
-
3 * 240000, enzyme from autotrophically grown cells, SDS-PAGE
trimer
Euglena gracilis 1224-5/9
-
3 * 240000, enzyme from autotrophically grown cells, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method. Crystallizes in space group P21 with four molecules per asymmetric unit. The 2.3 A resolution structure is solved by molecular replacement using the human cytosolic PCK
-
X-ray analysis, hanging-drop method
-
hanging drop vapour diffusion method using 0.1 M HEPES (pH 7.4) and 19% PEG 6000
P21642
enzyme alone and in complexes with the non-hydrolyzable GTP analog beta,gamma-methylene GTP, and with phosphoenolpyruvate, hanging-drop vapor-diffusion method, X-ray analysis
-
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
-
mutant enzyme A467G in complex with Mn2+, substrates and inhibitors
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
protein concentration 0.057 mg/ml, glutathione concentration 0.2 mM, stable for at least 3 h
80
-
Q6F494
half life: 53 min; half-life: 53 min
additional information
-
-
cytosolic enzyme is less stable against heat than mitochondrial enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol facilitates loss of activity
-
dithiothreitol stabilizes
-
photoinactivation by 8-azidoguanosine 5'-triphosphate
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PEPCK is very stable toward oxidative treatment
-
649936
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, 0.05 M potassium phosphate, pH 6.8, 0.2 M sucrose, stable for at least 21 months
-
4C, 3 weeks, stable
-
room temperature, at least 6 h, stable
-
4C, Co3+-PEPCK with Co3+ bound to enzyme at site n1, 1 week, stable
-
4C, Cr3+-PEPCK with Cr3+ bound to enzyme at site n1, at least 3 days, stable
-
4C, purified recombinant enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 1 month, 24% loss of activity
Q9AGJ6
4C, purified recombinant His-tagged enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 2 months, 25% loss of activity
Q9AGJ6
-15C, mitochondrial enzyme, stable for several months
-
4C, in absence of metal ions, under N2, protein concentration 0.5 mg/ml or higher, stable for at least 14 days
-
-20C, 0.2 M phosphate, DTT and glycerol, stable for 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type and mutant enzyme
-
recombinant and mutant enzyme
-
7.5fold, recombinant enzyme
-
recombinant enzyme
-
from autotrophically grown cells and heterotrophically grown cells
-
cytosolic enzyme
-
-
P35558
Ni-NTA Superflow agarose column chromatography and Ekapture-agarose column chromatography
-
recombinant enzyme
-
recombinant enzyme
Q9AGJ6
Superflow Ni2+-nitrilotriacetic acid-agarose chromatography
-
cytoslic and mitochondrial enzyme
-
glutathione-Uniflow resin column chromatography and P6DG column chromatography
-
recombinant enzyme
-
mutant PEP carboxykinase
P10963
; recombinant protein
Q6F494
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
wild-type and mutant PEPCK, expression in Escherichia coli 1786 and JM109
-
cytosolic and mitochondrial isoform of PEPCK, encoded by two different nuclear genes, expression in Escherichia coli XL1-B, sequencing
-
expression in Escherichia coli
-
pckA gene, overexpression in Escherichia coli HG89
-
expressed in Escherichia coli C41(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli, sequencing
-
expressed in Mus musculus
-
expressed in Escherichia coli C41(DE3) cells
-, Q9AGJ6
pck gene, overexpression in Escherichia coli C41(DE3), sequencing
Q9AGJ6
expressed in Escherichia coli HB101 cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli BL-21
-
mutant plasmid is transformed into the PEP carboxykinase-deficient yeast strain PUK-3B (MATalpha pck ura3)
P10963
expressed in Escherichia coli
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL
Q6F494
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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 with an IC50 of 2.3 mM
-
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
-
there is no effect of fish meal and fish oil substitution on hepatic levels of mitochondrial PEPCK mRNA
Q98T97
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
-
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
-
the pck mRNA level is higher when cells are grown on lactose than on glucose
-
higher expression levels under gluconeogenic conditions
Q6F494
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D262N
-
active site mutant, 5times higher catalytic efficiency than wild-type enzyme
D263N
-
increased Km-value for Mn2+ and phosphoenolpyruvate
H225Q
-
active site mutant, increased Km-value for Mn2+ and phosphoenolpyruvate
T249N
-
active site mutant
C306A
-
catalytically active mutant, kinetics
C306S
-
catalytically active mutant, kinetics
Y235A
P35558
site-directed mutagenesis
Y235F
P35558
site-directed mutagenesis
Y235S
P35558
site-directed mutagenesis
D75A
-, Q9AGJ6
75% reduced activity
D75N
-, Q9AGJ6
reduced activity
D75Q
-, Q9AGJ6
reduced activity
D75S
-, Q9AGJ6
reduced activity
D78A
-, Q9AGJ6
severely reduced activity
E83A
-, Q9AGJ6
severely reduced activity
S252A
P10963
side directed mutagenesis
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
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
potential target for anti-diabetic drugs
medicine
-
inhibitors of PEPCK may be useful in the treatment of type II diabetes
medicine
-
plays a role in the development of type 2 diabetes
pharmacology
-
orally active compounds reversibly inhibiting PEPCK improve glucose homeostasis in type 2 diabetics
pharmacology
-
development of a PEPCK inhibitor may lead to a new therapeutic strategy for the treatment of type II diabetes