BRENDA - Enzyme Database show
show all sequences of 1.1.1.87

Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug

Gabriel, I.; Vetter, N.D.; Palmer, D.R.; Milewska, M.J.; Wojciechowski, M.; Milewski, S.; FEMS Yeast Res. 13, 143-155 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of His-tagged enzyme in Escherichia coli strain TOP 10F'
Candida albicans
Inhibitors
Inhibitors
Commentary
Organism
Structure
(2R,3S)-3-(p-carboxybenzyl)malate
-
Candida albicans
(2S)-thiahomocitrate
-
Candida albicans
additional information
inhibitor docking study, molecular modeling of CaHIcDH-inhibitor interaction, overview
Candida albicans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
0.074
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.45
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
1.09
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
dependent on
Candida albicans
Mg2+
dependent on
Candida albicans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41491
-
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
42600
-
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
158000
-
gel filtration
Candida albicans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
Candida albicans
strict specificity for homoisocitrate
2-oxoadipate + CO2 + NADH + H+
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
Candida albicans ATCC 10231
strict specificity for homoisocitrate
2-oxoadipate + CO2 + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Candida albicans
-
gene LYS12
-
Candida albicans ATCC 10231
-
gene LYS12
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain TOP 10F by nickel affinity chromatography'
Candida albicans
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+
strict specificity for homoisocitrate
722303
Candida albicans
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
722303
Candida albicans
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate
722303
Candida albicans ATCC 10231
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
722303
Candida albicans ATCC 10231
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
additional information
substrate docking study
722303
Candida albicans
?
-
-
-
-
additional information
substrate docking study
722303
Candida albicans ATCC 10231
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
three-dimensional structure and homology modeling, overview
Candida albicans
tetramer
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Candida albicans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.38
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.38
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.4
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
0.4
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Candida albicans
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Candida albicans
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.000097
-
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
(2S)-thiahomocitrate
2.97
-
recombinant His-tagged enzyme, pH 7.8, 20°C, competitive versus (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Candida albicans
(2R,3S)-3-(p-carboxybenzyl)malate
3.78
-
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
(2R,3S)-3-(p-carboxybenzyl)malate
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of His-tagged enzyme in Escherichia coli strain TOP 10F'
Candida albicans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Candida albicans
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.000097
-
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
(2S)-thiahomocitrate
2.97
-
recombinant His-tagged enzyme, pH 7.8, 20°C, competitive versus (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Candida albicans
(2R,3S)-3-(p-carboxybenzyl)malate
3.78
-
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
(2R,3S)-3-(p-carboxybenzyl)malate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(2R,3S)-3-(p-carboxybenzyl)malate
-
Candida albicans
(2S)-thiahomocitrate
-
Candida albicans
additional information
inhibitor docking study, molecular modeling of CaHIcDH-inhibitor interaction, overview
Candida albicans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
0.074
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.45
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
1.09
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
dependent on
Candida albicans
Mg2+
dependent on
Candida albicans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41491
-
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
42600
-
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
158000
-
gel filtration
Candida albicans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
Candida albicans
strict specificity for homoisocitrate
2-oxoadipate + CO2 + NADH + H+
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
Candida albicans ATCC 10231
strict specificity for homoisocitrate
2-oxoadipate + CO2 + NADH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain TOP 10F by nickel affinity chromatography'
Candida albicans
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+
strict specificity for homoisocitrate
722303
Candida albicans
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
722303
Candida albicans
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate
722303
Candida albicans ATCC 10231
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
722303
Candida albicans ATCC 10231
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
additional information
substrate docking study
722303
Candida albicans
?
-
-
-
-
additional information
substrate docking study
722303
Candida albicans ATCC 10231
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
three-dimensional structure and homology modeling, overview
Candida albicans
tetramer
4 * 42600, SDS-PAGE, x * 41491, sequence calculation
Candida albicans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Candida albicans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.38
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.38
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.4
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
0.4
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Candida albicans
General Information
General Information
Commentary
Organism
additional information
three-dimensional structure and homology modeling, overview
Candida albicans
General Information (protein specific)
General Information
Commentary
Organism
additional information
three-dimensional structure and homology modeling, overview
Candida albicans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.35
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.44
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
5.16
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
8.75
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.35
-
NAD+
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
0.44
-
NAD+
native enzyme, pH 7.8, 20°C
Candida albicans
5.16
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
recombinant His-tagged enzyme, pH 7.8, 20°C
Candida albicans
8.75
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
native enzyme, pH 7.8, 20°C
Candida albicans
Other publictions for EC 1.1.1.87
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)
722303
Gabriel
Homoisocitrate dehydrogenase f ...
Candida albicans, Candida albicans ATCC 10231
FEMS Yeast Res.
13
143-155
2013
-
-
1
-
-
-
3
4
-
2
3
2
-
8
-
-
1
-
-
-
-
-
6
2
1
-
-
4
1
-
-
1
-
-
3
-
-
1
1
-
-
-
3
3
-
4
-
2
3
2
-
-
-
1
-
-
-
-
6
2
1
-
-
4
1
-
-
-
-
1
1
-
4
4
722569
Nango
Structure of Thermus thermophi ...
Thermus thermophilus
J. Biochem.
150
607-614
2011
-
-
-
1
-
-
2
1
-
1
-
1
-
5
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
1
-
-
-
-
-
1
1
-
-
-
2
1
1
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
690842
Takahashi
Characterization of key residu ...
Homo sapiens
Biochem. J.
419
113-122
2009
-
-
1
-
13
-
-
8
1
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
4
-
13
-
-
-
-
8
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692705
Farjo
RDH10 has 11-cis-retinol dehyd ...
Homo sapiens
Invest. Ophthalmol. Vis. Sci.
50
5089-5097
2009
1
-
1
-
-
-
-
-
-
-
-
2
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696350
Lin
Site-directed mutagenesis as a ...
Saccharomyces cerevisiae
Biochemistry
48
7305-7312
2009
-
-
-
-
2
-
-
1
-
2
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
2
1
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
2
1
-
-
-
-
-
-
-
-
685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
-
-
-
-
-
-
2
5
-
1
-
-
-
2
-
-
-
1
-
-
-
-
4
-
3
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
2
1
5
-
1
-
-
-
-
-
-
-
-
-
-
4
-
3
-
-
-
1
-
1
-
-
-
-
-
-
-
685539
Yamamoto
Thiahomoisocitrate: a highly p ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
16
3372-3376
2008
-
-
-
-
-
-
4
3
-
1
-
-
-
4
-
-
-
-
-
-
-
-
3
-
-
-
-
3
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
4
3
3
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
687735
Belyaeva
Kinetic analysis of human enzy ...
Homo sapiens
J. Biol. Chem.
283
20299-20308
2008
-
-
1
-
-
-
3
6
-
-
1
1
-
2
-
-
1
-
-
-
-
1
9
1
-
-
-
-
-
-
-
2
-
-
-
-
-
2
3
-
-
-
-
3
-
9
-
-
1
1
-
-
-
1
-
-
-
1
9
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687988
Romand
Dynamic expression of the reti ...
Mus musculus
J. Comp. Neurol.
508
879-892
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
-
-
-
-
-
-
4
3
-
5
-
1
-
2
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
1
-
1
1
-
-
-
-
-
1
-
-
-
-
4
1
3
-
5
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
667934
Yamamoto
Substrate specificity analysis ...
Deinococcus radiodurans, Saccharomyces cerevisiae
Bioorg. Med. Chem.
15
1346-1355
2007
-
-
1
-
-
-
11
20
-
2
-
-
-
7
-
-
1
-
-
-
2
-
24
-
2
-
-
20
2
-
-
2
9
-
-
-
-
1
2
-
-
-
-
11
9
20
-
2
-
-
-
-
-
1
-
-
2
-
24
-
2
-
-
20
2
-
-
-
-
-
-
-
-
-
686287
Cammas
Expression of the murine retin ...
Mus musculus
Dev. Dyn.
236
2899-2908
2007
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686950
Sandell
RDH10 is essential for synthes ...
Mus musculus
Genes Dev.
21
1113-1124
2007
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669670
Szamtari
PPARgamma controls CD1d expres ...
Homo sapiens
J. Exp. Med.
203
2351-2362
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
-
-
1
-
-
-
-
2
-
1
-
4
-
3
-
-
1
-
-
-
1
-
4
-
1
-
-
2
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
1
-
4
-
-
-
1
-
-
1
-
4
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
660918
Miyazaki
Identification of a novel trif ...
Deinococcus radiodurans
Biochem. Biophys. Res. Commun.
336
596-602
2005
-
-
1
-
4
-
-
7
-
2
2
-
-
4
-
-
1
-
-
-
1
-
3
1
1
-
-
7
1
-
-
1
-
-
-
-
-
1
1
-
4
-
-
-
-
7
-
2
2
-
-
-
-
1
-
-
1
-
3
1
1
-
-
7
1
-
-
-
-
-
-
-
-
-
669109
Miyazaki
Crystal structure of tetrameri ...
Thermus thermophilus
J. Bacteriol.
187
6779-6788
2005
-
-
-
1
1
-
-
2
-
1
-
-
-
2
-
-
-
-
-
-
1
-
3
1
1
-
-
2
1
-
-
1
-
-
-
-
-
-
1
1
1
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
1
-
3
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
656127
Miyazaki
Characterization of homoisocit ...
Thermus thermophilus
J. Biol. Chem.
278
1864-1871
2003
-
-
1
-
1
-
-
2
-
-
-
1
-
3
-
-
1
-
-
-
2
-
4
-
-
-
2
2
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
2
-
-
-
1
-
-
-
1
-
-
2
-
4
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
692332
Picozzi
Genomic organization and trans ...
Homo sapiens
FEBS Lett.
554
59-66
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692700
Wu
Cloning and characterization o ...
Bos taurus, Homo sapiens, Mus musculus
Invest. Ophthalmol. Vis. Sci.
43
3365-3372
2002
-
-
3
-
-
-
-
-
3
-
2
-
-
6
-
-
-
-
-
9
-
-
9
1
-
-
-
-
-
-
-
12
-
1
-
-
-
3
12
-
-
-
-
-
-
-
3
-
2
-
-
-
-
-
-
9
-
-
9
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
644538
Garrad
Lysine biosynthesis in selecte ...
Aspergillus fumigatus, Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisiae
J. Bacteriol.
174
7379-7384
1992
-
3
1
-
-
-
-
-
-
-
-
4
-
11
-
-
-
-
-
-
4
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288190
Ye
Lysine biosynthesis pathway an ...
Schizosaccharomyces pombe
J. Bacteriol.
170
5968-5970
1988
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
644540
Gaillardin
Wild-type and mutant forms of ...
Saccharomycopsis lipolytica
Eur. J. Biochem.
128
489-494
1982
-
-
-
-
-
2
3
-
-
3
1
1
-
3
-
-
1
-
-
-
1
2
2
2
1
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
2
-
3
-
-
-
3
1
1
-
-
-
1
-
-
1
2
2
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
644541
Broquist
-
Homoisocitric Dehydrogenase ...
Saccharomyces cerevisiae
Methods Enzymol.
17B
118-119
1971
-
-
-
-
-
-
-
1
-
1
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
644539
Rowley
Homoisocitric dehydrogenase fr ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
141
499-510
1970
2
-
-
-
-
-
1
4
-
3
1
1
-
2
-
-
1
-
-
-
1
-
3
-
1
-
-
-
2
2
-
2
-
-
-
2
-
-
2
-
-
-
-
1
-
4
-
3
1
1
-
-
-
1
-
-
1
-
3
-
1
-
-
-
2
2
-
-
-
-
-
-
-
-
644543
Strassmann
Enzymatic formation of alpha-k ...
Saccharomyces cerevisiae
J. Biol. Chem.
240
4357-4361
1965
-
-
-
-
-
-
-
1
-
1
-
1
-
1
-
-
1
-
-
-
-
2
2
-
1
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
2
2
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-