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Information on EC 2.7.11.5 - [Isocitrate dehydrogenase (NADP+)] kinase and Organism(s) Escherichia coli and UniProt Accession P11071

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IUBMB Comments
The enzyme has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate dehydrogenase (NADP+).
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This record set is specific for:
Escherichia coli
UNIPROT: P11071
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
isocitrate dehydrogenase kinase/phosphatase, idh kinase/phosphatase, idh kinase, idhk/p, idhkp, idh-k/p, icdh kinase/phosphatase, bifunctional isocitrate dehydrogenase kinase/phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isocitrate dehydrogenase kinase/phosphatase
-
bifunctional isocitrate dehydrogenase kinase/phosphatase
ICDH kinase/phosphatase
-
-
IDH kinase/phosphatase
-
-
IDH-K/P
-
-
isocitrate dehydrogenase kinase (phosphorylating)
-
-
-
-
isocitrate dehydrogenase kinase/phosphatase
[isocitrate dehydrogenase (NADP+)] kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
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
-
-
r
ATP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
ADP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
BsIDH is a much poorer substrate for the enzyme than EcIDH
-
-
?
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
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]N115L
ADP + [isocitrate dehydrogenase (NADP+)]N115L phosphate
show the reaction diagram
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]N15L
[isocitrate dehydrogenase (NADP+)]N15L phosphate
show the reaction diagram
-
-
-
-
?
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 + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
additional information
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
activates. Mn2+ and Mg2+ do not compete for the same binding site. Mn2+ appears to bind to the regulatory domain of AceK, and its effect is transmitted to the active site of the enzyme by the conformational change that it induces
additional information
-
Mn2+ or Ca2+ cannot replace Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
inhibits kinase activity
3-phosphoglycerate
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
8-azido-ATP
-
-
ADP
-
kinase hyperbolically inhibited
cupric 1,10 phenanthrolinate
-
-
DL-isocitrate
-
inhibits only kinase activity
glyoxylate
-
-
NADPH
oxaloacetate
-
inhibits kinase activity
phosphoenolpyruvate
-
kinase hyperbolically inhibited
pyruvate
[isocitrate dehydrogenase (NADP+)] phosphate
-
wild-type
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069 - 0.0147
ATP
0.016 - 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
-
pH 7.5, 37°C
-
0.0009
[isocitrate dehydrogenase (NADP+)]N15L
-
pH 7.5, 37°C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 20
3-phosphoglycerate
0.45
ADP
-
pH 7.3, 37°C
0.008 - 0.17
AMP
0.023
DL-isocitrate
-
pH 7.3, 37°C
0.011 - 0.016
isocitrate
0.042 - 0.082
NADPH
0.55
phosphoenolpyruvate
-
pH 7.3, 37°C
0.2 - 4
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11 - 0.63
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
kinase activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JM109
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
2 * 66000, homodimer, SDS-PAGE
130000
-
recombinant enzyme, gel filtration
135000
-
gel filtration, glycerol density gradient centrifugation
66000
68800
-
2 * 68800, homodimer, theoretical molecular mass
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 66000, homodimer, SDS-PAGE
?
x * 66000, SDS-PAGE
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D403A
site-directed mutagenesis
E439A
site-directed mutagenesis
N377A
site-directed mutagenesis
D475A
D477A
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
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
N462A
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 3 months
-
4°C, can be stored for several days without significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, bifunctional protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
aceK gene
-
aceK gene of Escherichia coli K-12 cloned in pQE30 expression vector to overproduce the protein in Escherichia coli JM105
-
bifunctional protein, expressed from the aceK gene
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expressed in Escherichia coli BL21(DE3) cells
recombinant wild-type IDHK/P on overproducing plasmid pJCD4, expressed in Escherichia coli JM109
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nimmo, G.A.; Borthwick, A.C.; Holms, W.H.; Nimmo, H.G.
Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308
Eur. J. Biochem.
141
401-408
1984
Escherichia coli
Manually annotated by BRENDA team
Nimmo, G.A.; Nimmo, H.G.
The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase
Eur. J. Biochem.
141
409-414
1984
Escherichia coli
Manually annotated by BRENDA team
Varela, I.; Nimmo, H.G.
Photoaffinity labelling shows that Escherichia coli isocitrate dehydrogenase kinase/phosphatase contains a single ATP-binding site
FEBS Lett.
231
361-365
1988
Escherichia coli, Escherichia coli KAT-1/pEM9
Manually annotated by BRENDA team
Ikeda, T.P.; Houtz, E.; LaPorte, D.C.
Isocitrate dehydrogenase kinase/phosphatase: identification of mutations which selectively inhibit phosphatase activity
J. Bacteriol.
174
1414-1416
1992
Escherichia coli, Escherichia coli W3550
Manually annotated by BRENDA team
Miller, S.P.; Karschnia, E.J.; Ikeda, T.P.; LaPorte, D.C.
Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins
J. Biol. Chem.
271
19124-19128
1996
Escherichia coli, Escherichia coli ST2010R
Manually annotated by BRENDA team
Rittinger, K.; Negre, D.; Divita, G.; Scarabel, M.; Bonod-Bidaud, C.; Goody, R.S.; Cozzone, A.J.; Cortay, J.C.
Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues
Eur. J. Biochem.
237
247-254
1996
Escherichia coli
Manually annotated by BRENDA team
El-Mansi, E.M.T.
Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli
FEMS Microbiol. Lett.
166
333-339
1998
Escherichia coli
Manually annotated by BRENDA team
Oudot, C.; Jaquinod, M.; Cortay, J.C.; Cozzone, A.J.; Jault, J.M.
The isocitrate dehydrogenase kinase/phosphatase from Escherichia coli is highly sensitive to in-vitro oxidative conditions role of cysteine67 and cysteine108 in the formation of a disulfide-bonded homodimer
Eur. J. Biochem.
262
224-229
1999
Escherichia coli, Escherichia coli JM109
Manually annotated by BRENDA team
Miller, S.P.; Chen, R.; Karschnia, E.J.; Romfo, C.; Dean, A.; LaPorte, D.C.
Locations of the regulatory sites for isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
275
833-839
2000
Escherichia coli
Manually annotated by BRENDA team
Oudot, C.; Cortay, J.C.; Blanchet, C.; Laporte, D.C.; Di Pietro, A.; Cozzone, A.J.; Jault, J.M.
The "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases
Biochemistry
40
3047-3055
2001
Escherichia coli (P11071), Escherichia coli, Escherichia coli JM109 (P11071)
Manually annotated by BRENDA team
Singh, S.K.; Matsuno, K.; LaPorte, D.C.; Banaszak, L.J.
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
276
26154-26163
2001
Escherichia coli
Manually annotated by BRENDA team
Singh, S.K.; Miller, S.P.; Dean, A.; Banaszak, L.J.; LaPorte, D.C.
Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
277
7567-7573
2002
Escherichia coli
Manually annotated by BRENDA team
Cozzone, A.J.; El-Mansi, M.
Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli
J. Mol. Microbiol. Biotechnol.
9
132-146
2005
Escherichia coli
Manually annotated by BRENDA team
Yates, S.P.; Edwards, T.E.; Bryan, C.M.; Stein, A.J.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.; Zheng, J.; Jia, Z.
Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase
Biochemistry
50
8103-8106
2011
Burkholderia pseudomallei (Q63Y16), Escherichia coli
Manually annotated by BRENDA team
Zheng, J.; Jia, Z.
Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase
Nature
465
961-965
2010
Escherichia coli (Q8X607), Escherichia coli, Escherichia coli 0157:H7 (Q8X607)
Manually annotated by BRENDA team
Zheng, J.; Yates, S.P.; Jia, Z.
Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK
Philos. Trans. R. Soc. Lond. B Biol. Sci.
367
2656-2668
2012
Escherichia coli
Manually annotated by BRENDA team
Yin, Y.; Li, S.; Gao, Y.; Tong, L.; Zheng, J.; Jia, Z.; Jiang, G.; Wei, Q.
Loopbeta3alphaC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase
FEBS Lett.
590
3144-3154
2016
Escherichia coli (P08200)
Manually annotated by BRENDA team
Song, P.; Wang, M.; Zheng, Q.; Wang, P.; Zhu, G.
Isocitrate dehydrogenase 1 from Acinetobacter baummanii (AbIDH1) enzymatic characterization and its regulation by phosphorylation
Biochimie
181
77-85
2021
Escherichia coli
Manually annotated by BRENDA team
Yin, Y.; Gao, Y.; Li, S.; Jiang, G.; Wei, Q.
Studies on the activation of isocitrate dehydrogenase kinase/phosphatase (AceK) by Mn2+ and Mg2
Biometals
31
991-1002
2018
Escherichia coli (Q8X607)
Manually annotated by BRENDA team