Information on EC 2.7.11.5 - [Isocitrate dehydrogenase (NADP+)] kinase

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
2.7.11.5
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RECOMMENDED NAME
GeneOntology No.
[Isocitrate dehydrogenase (NADP+)] kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase
The enzyme has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate dehydrogenase (NADP+).
CAS REGISTRY NUMBER
COMMENTARY hide
83682-93-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
Escherichia coli KAT-1/pEM9
KAT-1/pEM9
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Manually annotated by BRENDA team
ST2010R
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Manually annotated by BRENDA team
strain W3550 and mutants
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
ADP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
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BsIDH is a much poorer substrate for the enzyme than EcIDH
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?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
ATP + [isocitrate dehydrogenase (NADP+)]IS
ADP + [isocitrate dehydrogenase (NADP+)]IS phosphate
show the reaction diagram
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?
ATP + [isocitrate dehydrogenase (NADP+)]N115L
ADP + [isocitrate dehydrogenase (NADP+)]N115L phosphate
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
additional information
?
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AceK is a bifunctional enzyme, that phosphorylates and dephosphorylates isocitrate dehydrogenase with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Mn2+ or Ca2+ cannot replace Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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inhibits kinase activity
3-phosphoglycerate
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5,5'-dithio-bis(2-nitrobenzoic acid)
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8-azido-ATP
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ADP
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kinase hyperbolically inhibited
cupric 1,10 phenanthrolinate
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DL-isocitrate
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inhibits only kinase activity
glyoxylate
oxaloacetate
phosphoenolpyruvate
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kinase hyperbolically inhibited
pyruvate
[isocitrate dehydrogenase (NADP+)] phosphate
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wild-type
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069 - 0.32
ATP
0.0049 - 0.0582
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
0.00023 - 0.0059
[isocitrate dehydrogenase (NADP+)]
0.02
[isocitrate dehydrogenase (NADP+)]IS
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pH 7.5, 37C
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0.0009
[isocitrate dehydrogenase (NADP+)]N15L
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pH 7.5, 37C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 20
3-phosphoglycerate
0.45
ADP
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pH 7.3, 37C
0.008 - 0.17
AMP
0.023
DL-isocitrate
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pH 7.3, 37C
0.011 - 0.016
isocitrate
0.042 - 0.082
NADPH
0.55
phosphoenolpyruvate
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pH 7.3, 37C
0.2 - 4
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11 - 0.63
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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kinase activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
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recombinant enzyme, gel filtration
135000
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gel filtration, glycerol density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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reversible inactivation of the enzyme is due to reversible phosphorylation catalyzed by ICDH kinase/phosphatase. This activity requires ATP. Phosphorylation of the Ser113 residue renders the enzyme catalytically inactive as it prevents isocitrate from binding to the active site. This is a consequence of the negative charge carried on phosphoserine 113 and the conformational change associated with it. The ICDH molecule readily undergoes domain shift and/or induced-fit conformational changes to accomodate the binding changes of ICDH kinase/phosphatase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 3 months
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4C, can be stored for several days without significant loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, bifunctional protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aceK gene
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aceK gene of Escherichia coli K-12 cloned in pQE30 expression vector to overproduce the protein in Escherichia coli JM105
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bifunctional protein, expressed from the aceK gene
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recombinant wild-type IDHK/P on overproducing plasmid pJCD4, expressed in Escherichia coli JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D403A
site-directed mutagenesis
D477A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
E439A
site-directed mutagenesis
E478A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E497K/E499K
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
K291A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
K336A
site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
K346E
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
N377A
site-directed mutagenesis
N462A
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
D475A
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site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
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D477A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
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K291A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
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K336A
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site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
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N462A
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site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
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