BRENDA - Enzyme Database
show all sequences of 1.1.1.286

Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase

Miyazaki, K.; Biochem. Biophys. Res. Commun. 331, 341-346 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Pyrococcus horikoshii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0164
-
isocitrate
70°C, pH 7.8
Pyrococcus horikoshii
0.0183
-
homoisocitrate
70°C, pH 7.8
Pyrococcus horikoshii
0.0771
-
NAD+
70°C, pH 7.8
Pyrococcus horikoshii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
-
expression in Escherichia coli
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme expressed in Escherichia coli, purification of inclusion bodies requires N-laurylsarcosine
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NAD+
-
660907
Pyrococcus horikoshii
? + NADH
-
-
-
?
isocitrate + NAD+
about 20times more efficient than homoisocitrate, NAD+ is preferred over NADP+
660907
Pyrococcus horikoshii
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NADP+
NAD+ is preferred over NADP+
660907
Pyrococcus horikoshii
2-oxoglutarate + CO2 + NADPH
-
-
-
?
additional information
no substrate: 3-isopropylmalate
660907
Pyrococcus horikoshii
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.7
-
homoisocitrate
70°C, pH 7.8
Pyrococcus horikoshii
14.8
-
isocitrate
70°C, pH 7.8
Pyrococcus horikoshii
21.8
-
NAD+
70°C, pH 7.8
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus horikoshii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0164
-
isocitrate
70°C, pH 7.8
Pyrococcus horikoshii
0.0183
-
homoisocitrate
70°C, pH 7.8
Pyrococcus horikoshii
0.0771
-
NAD+
70°C, pH 7.8
Pyrococcus horikoshii
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme expressed in Escherichia coli, purification of inclusion bodies requires N-laurylsarcosine
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NAD+
-
660907
Pyrococcus horikoshii
? + NADH
-
-
-
?
isocitrate + NAD+
about 20times more efficient than homoisocitrate, NAD+ is preferred over NADP+
660907
Pyrococcus horikoshii
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NADP+
NAD+ is preferred over NADP+
660907
Pyrococcus horikoshii
2-oxoglutarate + CO2 + NADPH
-
-
-
?
additional information
no substrate: 3-isopropylmalate
660907
Pyrococcus horikoshii
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.7
-
homoisocitrate
70°C, pH 7.8
Pyrococcus horikoshii
14.8
-
isocitrate
70°C, pH 7.8
Pyrococcus horikoshii
21.8
-
NAD+
70°C, pH 7.8
Pyrococcus horikoshii
Other publictions for EC 1.1.1.286
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)
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8
1
1
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16
1
-
-
1
-
-
-
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-
1
1
1
6
-
-
-
-
32
-
1
-
4
-
-
-
1
-
-
-
-
8
1
1
-
-
16
1
-
-
-
-
3
3
-
31
31
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1
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-
-
-
2
-
-
-
6
-
5
-
-
1
-
-
-
-
-
6
1
1
-
-
2
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
-
-
6
-
-
-
1
-
-
-
-
6
1
1
-
-
2
1
-
-
-
-
1
1
-
2
2
740000
Takahashi
Determinants of dual substrate ...
Thermus thermophilus, Thermus thermophilus DSM 7039
Biochem. Biophys. Res. Commun.
478
1688-1693
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-
-
1
1
-
-
1
2
-
1
-
6
-
2
-
-
1
-
-
-
-
-
8
1
1
-
-
2
1
-
-
2
-
-
-
-
-
1
2
1
-
-
-
1
-
2
-
1
-
6
-
-
-
1
-
-
-
-
8
1
1
-
-
2
1
-
-
-
-
3
3
-
2
2
685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
-
-
-
-
-
-
3
1
-
-
-
1
-
1
-
-
-
2
-
-
-
-
3
-
1
-
-
-
1
1
-
1
1
-
-
-
-
-
1
-
-
-
-
3
1
1
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
-
-
-
-
-
-
4
-
-
4
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
3
-
-
-
-
-
1
-
-
-
-
4
3
-
-
4
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
-
-
1
-
-
-
-
3
-
-
-
-
-
3
-
-
1
-
-
-
-
-
4
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
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3
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
660918
Miyazaki
Identification of a novel trif ...
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Biochem. Biophys. Res. Commun.
336
596-602
2005
-
-
-
-
4
-
3
8
-
3
3
-
-
1
-
-
-
-
-
-
-
-
5
1
-
-
-
8
-
-
-
1
-
-
-
-
-
-
1
-
4
-
-
3
-
8
-
3
3
-
-
-
-
-
-
-
-
-
5
1
-
-
-
8
-
-
-
-
-
-
-
-
-
-
656127
Miyazaki
Characterization of homoisocit ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
J. Biol. Chem.
278
1864-1871
2003
-
-
1
-
1
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
6
1
-
-
1
2
-
-
-
-
-
-
-
-
-
1
-
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1
-
-
-
-
2
-
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6
1
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1
2
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