BRENDA - Enzyme Database
show all sequences of 1.1.1.286

Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae

Lin, Y.; Volkman, J.; Nicholas, K.M.; Yamamoto, T.; Eguchi, T.; Nimmo, S.L.; West, A.H.; Cook, P.F.; Biochemistry 47, 4169-4180 (2008)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
3-carboxypropylidenemalate
a dead-end inhibitor, competitive versus homoisocitrate
Saccharomyces cerevisiae
homoisocitrate
competitive, pH-dependent substrate inhibition
Saccharomyces cerevisiae
isocitrate
competitive, pH-dependent substrate inhibition
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic mechanism, detailed overview
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Saccharomyces cerevisiae
the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Reaction
Reaction
Commentary
Organism
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview
Saccharomyces cerevisiae
isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
chemical mechanism, stereochemistry of hydride transfer to NAD, overview
685232
Saccharomyces cerevisiae
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
rapid equilibrium random catalytic mechanism, stereochemistry of hydride transfer to NAD, overview
685232
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
additional information
the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent
685232
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH-profile, overview
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
stereochemistry of hydride transfer to NAD, overview
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.043
-
3-carboxypropylidenemalate
pH 8.0, 25°C, versus homoisocitrate
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
stereochemistry of hydride transfer to NAD, overview
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-carboxypropylidenemalate
a dead-end inhibitor, competitive versus homoisocitrate
Saccharomyces cerevisiae
homoisocitrate
competitive, pH-dependent substrate inhibition
Saccharomyces cerevisiae
isocitrate
competitive, pH-dependent substrate inhibition
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.043
-
3-carboxypropylidenemalate
pH 8.0, 25°C, versus homoisocitrate
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic mechanism, detailed overview
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Saccharomyces cerevisiae
the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
chemical mechanism, stereochemistry of hydride transfer to NAD, overview
685232
Saccharomyces cerevisiae
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
rapid equilibrium random catalytic mechanism, stereochemistry of hydride transfer to NAD, overview
685232
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
additional information
the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent
685232
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH-profile, overview
Saccharomyces cerevisiae
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)
740021
Shimizu
Structure and function of an a ...
Thermococcus kodakarensis, Thermococcus kodakarensis KRD1
Biochem. J.
474
105-122
2017
-
-
1
1
6
-
-
32
-
1
-
4
-
5
-
-
1
-
-
-
-
-
8
1
1
-
-
16
1
-
-
1
-
-
-
-
-
1
1
1
6
-
-
-
-
32
-
1
-
4
-
-
-
1
-
-
-
-
8
1
1
-
-
16
1
-
-
-
-
3
3
-
31
31
738195
Takahashi
Characterization of two ?-deca ...
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius MW001
Extremophiles
20
843-853
2016
-
-
1
-
-
-
-
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
2016
-
-
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
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
660918
Miyazaki
Identification of a novel trif ...
Deinococcus radiodurans
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
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
6
1
-
-
1
2
-
-
-
-
-
-
-
-
-
-