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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
2.7.11.5
-
RECOMMENDED NAME
GeneOntology No.
[Isocitrate dehydrogenase (NADP+)] kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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+).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AceK
Q8X607
-
AceK
Escherichia coli 0157:H7
Q8X607
-
-
bifunctional isocitrate dehydrogenase kinase/phosphatase
Q63Y16
-
bifunctional isocitrate dehydrogenase kinase/phosphatase
-
-
bifunctional isocitrate dehydrogenase kinase/phosphatase
Q8X607
-
bifunctional isocitrate dehydrogenase kinase/phosphatase
Escherichia coli 0157:H7
Q8X607
-
-
ICDH kinase/phosphatase
-
-
IDH kinase/phosphatase
-
-
IDH kinase/phosphatase
Escherichia coli KAT-1/pEM9, Escherichia coli W3550
-
-
-
IDH-K/P
-
-
IDHK/P
Escherichia coli JM109
-
-
-
isocitrate dehydrogenase kinase (phosphorylating)
-
-
-
-
isocitrate dehydrogenase kinase/phosphatase
-
-
isocitrate dehydrogenase kinase/phosphatase
Escherichia coli JM109
-
-
-
[isocitrate dehydrogenase (NADP+)] kinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
83682-93-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
K-12; ML308, ATCC 15224
-
-
Manually annotated by BRENDA team
KAT-1/pEM9
-
-
Manually annotated by BRENDA team
ML308, ATCC 15224
-
-
Manually annotated by BRENDA team
ST2010R
-
-
Manually annotated by BRENDA team
strain W3550 and mutants
-
-
Manually annotated by BRENDA team
Escherichia coli 0157:H7
-
UniProt
Manually annotated by BRENDA team
Escherichia coli JM109
JM109
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
JM109
Uniprot
Manually annotated by BRENDA team
Escherichia coli KAT-1/pEM9
KAT-1/pEM9
-
-
Manually annotated by BRENDA team
Escherichia coli ST2010R
ST2010R
-
-
Manually annotated by BRENDA team
Escherichia coli W3550
strain W3550 and mutants
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria
evolution
Q8X607
AceK is significantly larger than typical eukaryotic protein kinases. Apart from the ATP-binding motif, AceK does not share sequence homology with any eukaryotic protein kinase or phosphatase
evolution
-
the N-terminal domain or regulatory domain of AceK represents a unique protein fold with no structural homologues All known and putative AceK proteins exist only in Gram-negative bacteria, close evolutionary relationship among Gram-negative bacterial AceK-IDH systems
evolution
Escherichia coli 0157:H7
-
AceK is significantly larger than typical eukaryotic protein kinases. Apart from the ATP-binding motif, AceK does not share sequence homology with any eukaryotic protein kinase or phosphatase
-
metabolism
Q8X607
Escherichia coli isocitrate dehydrogenase kinase/phosphatase is a unique bifunctional enzyme that phosphorylates or dephosphorylates isocitrate dehydrogenase, ICDH, in response to environmental changes, resulting in the inactivation or, respectively, activation of ICDH1. ICDH inactivation short-circuits the Krebs cycle by enabling the glyoxlate bypass
metabolism
-
AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation, pathway overview
physiological function
-
isocitrate dehydrogenase kinase/phosphatase, AceK, regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase, ICDH
physiological function
-
AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation
metabolism
Escherichia coli 0157:H7
-
Escherichia coli isocitrate dehydrogenase kinase/phosphatase is a unique bifunctional enzyme that phosphorylates or dephosphorylates isocitrate dehydrogenase, ICDH, in response to environmental changes, resulting in the inactivation or, respectively, activation of ICDH1. ICDH inactivation short-circuits the Krebs cycle by enabling the glyoxlate bypass
-
additional information
Q8X607
structures of AceK and its complex with ICDH. AceK contains a eukaryotic protein-kinase-like domain containing ATP and a regulatory domain with a distinct fold. AMP-mediated conformational change exposes and shields ATP, acting as a switch between AceK kinase and phosphatase activities, and ICDH-binding induces further conformational change for AceK activation. The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH, structure-based recognition of Asp 477 being located at the ATP-binding site
additional information
-
AceK and its complex with its protein substrate isocitrate dehydrogenase, IDH, interaction analysis, overview. Asp457-Asn462-Asp475 catalytic triad. In addition to this catalytic element, a phosphotransferase motif is also evident in AceK with sequence is 455PGDMLFKNFGV465. One of the most striking differences between AceK and the eukaryotic protein kinases family is the presence of loop beta3aalphaC in AceK. This regulatory loop shields and exposes ATP in the AMP-bound and AMP-free AceK structures, respectively, thereby acting as a regulator of catalytic function as it controls the accessibility to the ATP binding site. The regulatory domain of AceK contains binding pockets for small molecules that can regulate the function of the catalytic kinase domain of AceK
additional information
Escherichia coli 0157:H7
-
structures of AceK and its complex with ICDH. AceK contains a eukaryotic protein-kinase-like domain containing ATP and a regulatory domain with a distinct fold. AMP-mediated conformational change exposes and shields ATP, acting as a switch between AceK kinase and phosphatase activities, and ICDH-binding induces further conformational change for AceK activation. The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH, structure-based recognition of Asp 477 being located at the ATP-binding site
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
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+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
-
-
r
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
-
-
-
r
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
-
-
-
r
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
-
-
-
r
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
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
P11071
-
-
r
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
-
-
-
r
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
Q63Y16
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Q8X607
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
Ser113 from Escherichia coli class A ICDH is the target of phosphorylation by AceK and is structurally conserved among all ICDHs. Burkholderia pseudomallei class A ICDH also exhibits the necessary structural elements required for Escherichia coli AceK recognition
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Q8X607
The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli JM109
-
-, controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli W3550
-
-, reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli KAT-1/pEM9
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli ST2010R
-
-, reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli 0157:H7
Q8X607
-, The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH
-
-
r
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
-
-
-
-
?
additional information
?
-
-
uses only ATP, no other nucleoside triphospates as only very poor phosphate donors for the kinase activity, GTP and UTP can activate the phosphatase activity to some extent
-
-
-
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, AceK exhibits ATPase activity
-
-
-
additional information
?
-
-
AceK kinase assay is coupled to ICDH activity, whereby the reduction of NADP+ to NADPH is monitored. When AceK phosphorylates ICDH, the activity of ICDH is inhibited. Structure comparisons of Burkholderia pseudomallei ICDH and Echerichia coli ICDH substrates, overview. Bacillus subtilis ICDH and Acidithiobacillus thiooxidans ICDH are poor substrates for AceK
-
-
-
additional information
?
-
Escherichia coli, Escherichia coli 0157:H7
Q8X607
bifunctional AceK possesses the two opposing activities of protein kinase and phosphatase within one protein, and specifically recognizes only intact ICDH. Additionally, AceK has strong ATPase activity
-
-
-
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
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
-
-
-
r
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
-
-
-
r
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
P11071
-
-
r
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
Q63Y16
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Q8X607
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
-
Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli JM109
-
controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli W3550
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli KAT-1/pEM9
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli ST2010R
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
show the reaction diagram
Escherichia coli 0157:H7
Q8X607
-
-
-
r
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
ADP
-
AceK is strictly ATP/ADP-dependent
ATP
-
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
ATP
Q8X607
ATP-binding site, structure modeling, overview
ATP
-
AceK is strictly ATP/ADP-dependent. Conserved Lys336 in the ATP binding site interacts with and stabilizes the alpha-phosphate of enzyme-bound ATP
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
absolute requirement, isocitrate dehydrogenase phosphatase responds hyperbolically to Mg2+ ions
Mg2+
P11071
-
Mg2+
Q63Y16
required
Mg2+
-
required
Mg2+
-
required, only one Mg2 is found in AceK, whereas two are present in ePKs
additional information
-
Mn2+ or Ca2+ cannot replace Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
inhibits kinase activity
3-phosphoglycerate
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
8-azido-ATP
-
-
ADP
-
kinase hyperbolically inhibited
AMP
-
kinase hyperbolically inhibited
AMP
Q8X607
acts as an AceK phosphatase activator and kinase inhibitor, AMP binds in an allosteric site between the two AceK domains, allosteric AMP-binding site, structure modeling, overview
cupric 1,10 phenanthrolinate
-
-
DL-isocitrate
-
inhibits only kinase activity
glyoxylate
-
in combination with oxaloacetate
NADPH
-
inhibits both IDH kinase and IDH phosphatase
oxaloacetate
-
inhibits kinase activity
phosphoenolpyruvate
-
kinase hyperbolically inhibited
pyruvate
-
inhibits kinase activity
[isocitrate dehydrogenase (NADP+)] phosphate
-
wild-type
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0069
-
ATP
P11071
pH 7.5, 37C, wild-type
0.0087
-
ATP
P11071
pH 7.5, 37C, mutant D403A
0.0098
-
ATP
P11071
pH 7.5, 37C, mutant Glu439Ala
0.0147
-
ATP
P11071
pH 7.5, 37C, mutant Asn377Ala
0.016
-
ATP
-
pH 7.5, 37C, wild-type, kinase activity
0.088
-
ATP
-
pH 7.3, 37C
0.1
-
ATP
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.32
-
ATP
-
pH 7.5, 37C, mutant AceK4, kinase activity
0.0049
-
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C
-
0.0582
-
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C, kinase activity at saturating ATP
-
0.00023
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C, wild-type and mutant AceK4, kinase activity
0.00025
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.00035
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.3, 37C, kinase activity
0.00078
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C, kinase activity at saturating ATP
0.0017
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C
0.0059
-
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37C
0.02
-
[isocitrate dehydrogenase (NADP+)]IS
-
pH 7.5, 37C
-
0.0009
-
[isocitrate dehydrogenase (NADP+)]N15L
-
pH 7.5, 37C
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
3-phosphoglycerate
-
pH 7.5, 37C, wild-type, kinase activity
4
-
3-phosphoglycerate
-
pH 7.5, 37C, mutant AceK4, kinase activity
20
-
3-phosphoglycerate
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.45
-
ADP
-
pH 7.3, 37C
0.008
-
AMP
-
pH 7.5, 37C
0.02
-
AMP
-
pH 7.5, 37C, mutant AceK4, kinase activity
0.056
-
AMP
-
pH 7.3, 37C
0.17
-
AMP
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.023
-
DL-isocitrate
-
pH 7.3, 37C
0.011
-
Isocitrate
-
pH 7.5, 37C, mutant AceK4, kinase activity
0.015
-
Isocitrate
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.016
-
Isocitrate
-
pH 7.5, 37C, wild-type, kinase activity
0.042
-
NADPH
-
pH 7.3, 37C
0.058
-
NADPH
-
pH 7.5, 37C, mutant AceK4, kinase activity
0.073
-
NADPH
-
pH 7.5, 37C, mutant AceK3, kinase activity
0.082
-
NADPH
-
pH 7.5, 37C, wild-type, kinase activity
0.55
-
phosphoenolpyruvate
-
pH 7.3, 37C
0.2
-
pyruvate
-
pH 7.5, 37C, wild-type, kinase activity
1
-
pyruvate
-
pH 7.5, 37C, mutant AceK4, kinase activity
4
-
pyruvate
-
pH 7.5, 37C, mutant AceK3, kinase activity
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.038
-
-
-
0.11
0.63
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
8.5
-
kinase activity
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65000
-
Q8X607
-
130000
-
-
recombinant enzyme, gel filtration
135000
-
-
gel filtration, glycerol density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 66000, homodimer, SDS-PAGE; 2 * 68800, homodimer, theoretical molecular mass
dimer
-
2 * 66000, homodimer, SDS-PAGE
dimer
Escherichia coli JM109
-
2 * 66000, homodimer, SDS-PAGE; 2 * 68800, homodimer, theoretical molecular mass
-
additional information
Q8X607
architecture of the AceK structure as both a kinase domain and a regulatory domain. The domains exist as an inactive protein complex of a catalytic subunit and a regulatory subunit. Although the regulatory subunit is a separate protein, its binding of ligands facilitates activation of the catalytic subunit
additional information
Escherichia coli 0157:H7
-
architecture of the AceK structure as both a kinase domain and a regulatory domain. The domains exist as an inactive protein complex of a catalytic subunit and a regulatory subunit. Although the regulatory subunit is a separate protein, its binding of ligands facilitates activation of the catalytic subunit
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 3 months
-
4C, can be stored for several days without significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial, bifunctional protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
recombinant wild-type IDHK/P on overproducing plasmid pJCD4, expressed in Escherichia coli JM109
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D403A
P11071
site-directed mutagenesis
D475A
Q8X607
site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
D475A
-
the mutation in this signature motif completely abolishes kinase activity of the enzyme
D477A
Q8X607
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
E439A
P11071
site-directed mutagenesis
E478A
Q8X607
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E497K/E499K
Q8X607
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
K291A
Q8X607
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
K336A
Q8X607
site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
K346E
Q8X607
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
N377A
P11071
site-directed mutagenesis
N462A
Q8X607
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
D475A
Escherichia coli 0157:H7
-
site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
-
D477A
Escherichia coli 0157:H7
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
-
K291A
Escherichia coli 0157:H7
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
K336A
Escherichia coli 0157:H7
-
site-directed mutagenesis, the mutant shows completely reduced activity compared to the wild-type enzyme
-
N462A
Escherichia coli 0157:H7
-
site-directed mutagenesis, the mutant shows about 75% reduced activity compared to the wild-type enzyme
-