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Information on EC 4.1.1.49 - phosphoenolpyruvate carboxykinase (ATP) and Organism(s) Trypanosoma cruzi and UniProt Accession P51058

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.49 phosphoenolpyruvate carboxykinase (ATP)
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This record set is specific for:
Trypanosoma cruzi
UNIPROT: P51058 not found.
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The taxonomic range for the selected organisms is: Trypanosoma cruzi
The enzyme appears in selected viruses and cellular organisms
Synonyms
pepc kinase, protein p60, phosphoenolpyruvate carboxylase kinase, pepk, atp-dependent phosphoenolpyruvate carboxykinase, pep carboxylase kinase, osppck3, pfpepck, osppck1, pepck (atp), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:oxaloacetate carboxylyase (transphosphorylating)
-
phosphoenolpyruvate carboxykinase
-
ATP-oxaloacetate carboxylase (transphosphorylating)
-
-
Carboxykinase, phosphopyruvate (adenosine triphosphate)
-
-
-
-
Glycosomal protein P60
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxylase
-
-
-
-
PEPCK
-
-
-
-
PEPCK (ATP)
-
-
-
-
PEPK
-
-
-
-
phosphoenolpyruvate carboxykinase
Phosphoenolpyruvate carboxylase
-
-
-
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Phosphoenolpyruvate carboxylase (ATP)
-
-
-
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phosphoenolpyruvic carboxykinase
-
-
-
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Phosphoenolpyruvic carboxylase
-
-
-
-
phosphopyruvate carboxykinase
-
-
-
-
Phosphopyruvate carboxykinase (adenosine triphosphate)
-
-
-
-
Protein p60
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9073-94-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
CTP + oxaloacetate
CDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
15% of the activity with ATP
-
-
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
52% of the activity with ATP
-
-
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
36% of the activity with ATP
-
-
?
TTP + oxaloacetate
TDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
16% of the activity with ATP
-
-
?
UTP + oxaloacetate
UDP + phosphoenolpyruvate + CO2
show the reaction diagram
-
20% of the activity with ATP
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
-
first commmitted step of gluconeogenesis
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
exchange reaction: Mn2+ is the most effective divalent cation activator followed by Cd2+ and Mg2+
Mg2+
-
exchange reaction: MnCl2 is the most effective divalent cation activator followed by Cd2+ and Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Mercaptopicolinic acid
-
specific to this enzyme
5,5'-dithiobis(2-nitrobenzoate)
-
-
Fluorescein mercuric acetate
-
-
IDP
-
inhibits exchange reaction with ATP or GTP
o-Iodosobenzoate
-
0.5 mM, 50% inhibition
oxalate
-
competitive inhibitor
p-chloromercuribenzenesulfonate
-
-
p-chloromercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 0.039
ADP
0.019 - 0.027
ATP
3.7
CO2
-
CO2 in form of HCO3-
0.027 - 0.044
oxaloacetate
0.035 - 0.36
phosphoenolpyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
o-Iodosobenzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
carboxylation
8
-
decarboxylation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PCKA_TRYCR
472
0
52585
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
2 * 42000, SDS-PAGE
52500
-
x * 52500, calculation from nucleotide sequence
82000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52500, calculation from nucleotide sequence
dimer
-
2 * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion, primitive orthorhombic crystals, space group P2(1)2(1)2(1), a : 65.97 A, b : 107.61 A, c : 179.08 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Trypanosoma cruzi is the causative agent of Chagas' disease, enzyme is a good target for the development of new anti-chagasic drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Urbina, J.A.
The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: molecular, kinetic, and regulatory properties
Arch. Biochem. Biophys.
258
186-195
1987
Trypanosoma cruzi
Manually annotated by BRENDA team
Linss, J.; Goldenberg, S.; Urbina, J.A.; Amzel, L.M.
Cloning and characterization of the gene encoding ATP-dependent phospho-enol-pyruvate carboxykinase in Trypanosoma cruzi: comparison of primary and predicted secondary structure with host GTP-dependent enzyme
Gene
136
69-77
1993
Trypanosoma cruzi
Manually annotated by BRENDA team
Urbina, J.A.; Orsono, C.E.; Rojas, A.
Inhibition of phosphoenolpyruvate carboxykinase from Trypanosoma (Schizotrypanum) cruzi epimastigotes by 3-mercaptopicolinic acid: in vitro and in vivo studies
Arch. Biochem. Biophys.
282
91-99
1990
Trypanosoma cruzi
Manually annotated by BRENDA team
Cymeryng, C.; Cazzulo, J.J.; Cannata, J.J.B.
Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
Mol. Biochem. Parasitol.
73
91-101
1995
Trypanosoma cruzi, Trypanosoma cruzi Tul O
Manually annotated by BRENDA team
Delbaere, L.T.J.; Sudom, A.M.; Prasad, L.; Leduc, Y.; Goldie, H.
Structure/function studies of phosphoryl transfer by phosphoenolpyruvate carboxykinase
Biochim. Biophys. Acta
1697
271-278
2004
Corynebacterium glutamicum, Escherichia coli, Trypanosoma cruzi
Manually annotated by BRENDA team
Trapani, S.; Linss, J.; Goldenberg, S.; Fischer, H.; Craievich, A.F.; Oliva, G.
Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 A resolution
J. Mol. Biol.
313
1059-1072
2001
Trypanosoma cruzi (P51058), Trypanosoma cruzi
Manually annotated by BRENDA team