BRENDA - Enzyme Database
show all sequences of 2.7.11.5

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

Nimmo, G.A.; Nimmo, H.G.; Eur. J. Biochem. 141, 409-414 (1984)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
inhibits kinase activity
Escherichia coli
ADP
kinase hyperbolically inhibited
Escherichia coli
AMP
kinase hyperbolically inhibited
Escherichia coli
DL-isocitrate
inhibits only kinase activity
Escherichia coli
glyoxylate
-
Escherichia coli
NADPH
-
Escherichia coli
oxaloacetate
inhibits kinase activity
Escherichia coli
phosphoenolpyruvate
kinase hyperbolically inhibited
Escherichia coli
pyruvate
inhibits kinase activity
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00035
-
[isocitrate dehydrogenase (NADP+)]
pH 7.3, 37°C, kinase activity
Escherichia coli
0.088
-
ATP
pH 7.3, 37°C
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolute requirement, isocitrate dehydrogenase phosphatase responds hyperbolically to Mg2+ ions
Escherichia coli
additional information
Mn2+ or Ca2+ cannot replace Mg2+
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + [isocitrate dehydrogenase (NADP+)]
Escherichia coli
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
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
Escherichia coli
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
ML308, ATCC 15224
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + [isocitrate dehydrogenase (NADP+)]
-
640602
Escherichia coli
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
640602
Escherichia coli
r
ATP + [isocitrate dehydrogenase (NADP+)]
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
640602
Escherichia coli
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
640602
Escherichia coli
r
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
640602
Escherichia coli
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.5
kinase activity
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
ADP
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
Escherichia coli
ATP
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
Escherichia coli
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.023
-
DL-isocitrate
pH 7.3, 37°C
Escherichia coli
0.042
-
NADPH
pH 7.3, 37°C
Escherichia coli
0.056
-
AMP
pH 7.3, 37°C
Escherichia coli
0.45
-
ADP
pH 7.3, 37°C
Escherichia coli
0.55
-
phosphoenolpyruvate
pH 7.3, 37°C
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ADP
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
Escherichia coli
ATP
isocitrate dehydrogenase phosphatase requires a nucleotide for activity
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
inhibits kinase activity
Escherichia coli
ADP
kinase hyperbolically inhibited
Escherichia coli
AMP
kinase hyperbolically inhibited
Escherichia coli
DL-isocitrate
inhibits only kinase activity
Escherichia coli
glyoxylate
-
Escherichia coli
NADPH
-
Escherichia coli
oxaloacetate
inhibits kinase activity
Escherichia coli
phosphoenolpyruvate
kinase hyperbolically inhibited
Escherichia coli
pyruvate
inhibits kinase activity
Escherichia coli
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.023
-
DL-isocitrate
pH 7.3, 37°C
Escherichia coli
0.042
-
NADPH
pH 7.3, 37°C
Escherichia coli
0.056
-
AMP
pH 7.3, 37°C
Escherichia coli
0.45
-
ADP
pH 7.3, 37°C
Escherichia coli
0.55
-
phosphoenolpyruvate
pH 7.3, 37°C
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00035
-
[isocitrate dehydrogenase (NADP+)]
pH 7.3, 37°C, kinase activity
Escherichia coli
0.088
-
ATP
pH 7.3, 37°C
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolute requirement, isocitrate dehydrogenase phosphatase responds hyperbolically to Mg2+ ions
Escherichia coli
additional information
Mn2+ or Ca2+ cannot replace Mg2+
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + [isocitrate dehydrogenase (NADP+)]
Escherichia coli
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
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
Escherichia coli
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + [isocitrate dehydrogenase (NADP+)]
-
640602
Escherichia coli
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
640602
Escherichia coli
r
ATP + [isocitrate dehydrogenase (NADP+)]
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
640602
Escherichia coli
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
640602
Escherichia coli
r
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
640602
Escherichia coli
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.5
kinase activity
Escherichia coli
Other publictions for EC 2.7.11.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738248
Yin
Loopbeta3alphaC plays an impor ...
Escherichia coli
FEBS Lett.
590
3144-3154
2016
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723346
Zheng
Structural and mechanistic ins ...
Escherichia coli
Philos. Trans. R. Soc. Lond. B Biol. Sci.
367
2656-2668
2012
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4
4
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721649
Yates
Structural basis of the substr ...
Burkholderia pseudomallei, Escherichia coli
Biochemistry
50
8103-8106
2011
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2
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723265
Zheng
Structure of the bifunctional ...
Escherichia coli 0157:H7, Escherichia coli
Nature
465
961-965
2010
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8
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1
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2
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4
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6
1
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1
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8
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1
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1
2
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6
1
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3
3
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666105
Cozzone
Control of isocitrate dehydrog ...
Escherichia coli
J. Mol. Microbiol. Biotechnol.
9
132-146
2005
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-
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2
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1
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640612
Singh
Bacillus subtilis isocitrate d ...
Escherichia coli
J. Biol. Chem.
277
7567-7573
2002
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640610
Oudot
The 'catalytic' triad of isoci ...
Escherichia coli, Escherichia coli JM109
Biochemistry
40
3047-3055
2001
-
-
-
-
3
-
-
4
-
1
1
1
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3
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1
1
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640611
Singh
Crystal structure of Bacillus ...
Escherichia coli
J. Biol. Chem.
276
26154-26163
2001
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640609
Miller
Locations of the regulatory si ...
Escherichia coli
J. Biol. Chem.
275
833-839
2000
-
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5
3
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1
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2
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3
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15
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5
15
3
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3
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640608
Oudot
The isocitrate dehydrogenase k ...
Escherichia coli, Escherichia coli JM109
Eur. J. Biochem.
262
224-229
1999
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1
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2
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2
2
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32
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2
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640607
El-Mansi
Control of metabolic interconv ...
Escherichia coli
FEMS Microbiol. Lett.
166
333-339
1998
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640605
Miller
Isocitrate dehydrogenase kinas ...
Escherichia coli, Escherichia coli ST2010R
J. Biol. Chem.
271
19124-19128
1996
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640606
Rittinger
Escherichia coli isocitrate de ...
Escherichia coli
Eur. J. Biochem.
237
247-254
1996
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640604
Ikeda
Isocitrate dehydrogenase kinas ...
Escherichia coli, Escherichia coli W3550
J. Bacteriol.
174
1414-1416
1992
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640603
Varela
Photoaffinity labelling shows ...
Escherichia coli, Escherichia coli KAT-1/pEM9
FEBS Lett.
231
361-365
1988
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640601
Nimmo
Partial purification and prope ...
Escherichia coli
Eur. J. Biochem.
141
401-408
1984
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640602
Nimmo
The regulatory properties of i ...
Escherichia coli
Eur. J. Biochem.
141
409-414
1984
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2
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5
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5
2
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3
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1
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640600
Wang
The reversible phosphorylation ...
Salmonella enterica subsp. enterica serovar Typhimurium
Arch. Biochem. Biophys.
218
59-67
1982
4
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