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show all sequences of 1.1.1.87

Identification of a novel trifunctional homoisocitrate dehydrogenase and modulation of the broad substrate specificity through site-directed mutagenesis

Miyazaki, K.; Biochem. Biophys. Res. Commun. 336, 596-602 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain OM17
Deinococcus radiodurans
Engineering
Amino acid exchange
Commentary
Organism
A80del
site-directed mutagenesis, the mutant shows altered substrate specificity preferring isocitrate to homoisocitrate, it is unable to oxidize 3-isopropylmalate, the specificity is similar to the enzyme from Thermus thermophilus
Deinococcus radiodurans
additional information
modulation of the broad substrate specificity of the trifunctional enzyme through site-directed mutagenesis, overview
Deinococcus radiodurans
R87T
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
Deinococcus radiodurans
R87V
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
Deinococcus radiodurans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.211
-
homoisocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
0.291
-
isocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
0.465
-
isocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
0.819
-
homoisocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
1
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87V
Deinococcus radiodurans
1.33
-
3-isopropylmalate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
1.5
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87T
Deinococcus radiodurans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
required
Deinococcus radiodurans
Mn2+
required
Deinococcus radiodurans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
4 * 40000, recombinant enzyme, SDS-PAGE
Deinococcus radiodurans
154000
-
recombinant enzyme, gel filtration
Deinococcus radiodurans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Deinococcus radiodurans
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain OM17 by anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography
Deinococcus radiodurans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Deinococcus radiodurans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-isopropylmalate + NAD+
-
660918
Deinococcus radiodurans
?
-
-
-
?
homoisocitrate + NAD+
1.5fold preferred to isocitrate
660918
Deinococcus radiodurans
?
-
-
-
?
isocitrate + NAD+
-
660918
Deinococcus radiodurans
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 40000, recombinant enzyme, SDS-PAGE
Deinococcus radiodurans
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Deinococcus radiodurans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.371
-
3-isopropylmalate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
5.46
-
homoisocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
10.9
-
isocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
20.8
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87V
Deinococcus radiodurans
27.8
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87T
Deinococcus radiodurans
42.8
-
isocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
46.2
-
homoisocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Deinococcus radiodurans
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Deinococcus radiodurans
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain OM17
Deinococcus radiodurans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Deinococcus radiodurans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A80del
site-directed mutagenesis, the mutant shows altered substrate specificity preferring isocitrate to homoisocitrate, it is unable to oxidize 3-isopropylmalate, the specificity is similar to the enzyme from Thermus thermophilus
Deinococcus radiodurans
additional information
modulation of the broad substrate specificity of the trifunctional enzyme through site-directed mutagenesis, overview
Deinococcus radiodurans
R87T
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
Deinococcus radiodurans
R87V
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
Deinococcus radiodurans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.211
-
homoisocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
0.291
-
isocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
0.465
-
isocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
0.819
-
homoisocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
1
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87V
Deinococcus radiodurans
1.33
-
3-isopropylmalate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
1.5
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87T
Deinococcus radiodurans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
required
Deinococcus radiodurans
Mn2+
required
Deinococcus radiodurans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
4 * 40000, recombinant enzyme, SDS-PAGE
Deinococcus radiodurans
154000
-
recombinant enzyme, gel filtration
Deinococcus radiodurans
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain OM17 by anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography
Deinococcus radiodurans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Deinococcus radiodurans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-isopropylmalate + NAD+
-
660918
Deinococcus radiodurans
?
-
-
-
?
homoisocitrate + NAD+
1.5fold preferred to isocitrate
660918
Deinococcus radiodurans
?
-
-
-
?
isocitrate + NAD+
-
660918
Deinococcus radiodurans
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 40000, recombinant enzyme, SDS-PAGE
Deinococcus radiodurans
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Deinococcus radiodurans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.371
-
3-isopropylmalate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
5.46
-
homoisocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
10.9
-
isocitrate
pH 7.8, 25C, recombinant mutant A80del
Deinococcus radiodurans
20.8
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87V
Deinococcus radiodurans
27.8
-
homoisocitrate
pH 7.8, 25C, recombinant mutant R87T
Deinococcus radiodurans
42.8
-
isocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
46.2
-
homoisocitrate
pH 7.8, 25C, recombinant wild-type enzyme
Deinococcus radiodurans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Deinococcus radiodurans
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
-
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1
-
-
-
3
4
-
2
3
2
-
8
-
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1
-
-
-
-
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6
2
1
-
-
4
1
-
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1
-
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3
-
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1
1
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3
3
-
4
-
2
3
2
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1
-
-
-
-
6
2
1
-
-
4
1
-
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1
1
-
4
4
722569
Nango
Structure of Thermus thermophi ...
Thermus thermophilus
J. Biochem.
150
607-614
2011
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1
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2
1
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1
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1
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5
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2
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1
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1
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1
1
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1
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1
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1
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2
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1
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1
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1
1
-
-
-
690842
Takahashi
Characterization of key residu ...
Homo sapiens
Biochem. J.
419
113-122
2009
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-
1
-
13
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8
1
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1
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13
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1
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2
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692705
Farjo
RDH10 has 11-cis-retinol dehyd ...
Homo sapiens
Invest. Ophthalmol. Vis. Sci.
50
5089-5097
2009
1
-
1
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2
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4
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4
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696350
Lin
Site-directed mutagenesis as a ...
Saccharomyces cerevisiae
Biochemistry
48
7305-7312
2009
-
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-
-
2
-
-
1
-
2
-
1
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2
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2
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1
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2
1
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1
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1
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2
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1
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2
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1
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2
-
1
-
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-
2
1
-
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685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
-
-
-
-
-
-
2
5
-
1
-
-
-
2
-
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1
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-
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4
-
3
-
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-
1
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1
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1
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-
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2
1
5
-
1
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-
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-
4
-
3
-
-
-
1
-
1
-
-
-
-
-
-
-
685539
Yamamoto
Thiahomoisocitrate: a highly p ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
16
3372-3376
2008
-
-
-
-
-
-
4
3
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1
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4
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3
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3
1
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3
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4
3
3
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1
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3
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3
1
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687735
Belyaeva
Kinetic analysis of human enzy ...
Homo sapiens
J. Biol. Chem.
283
20299-20308
2008
-
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1
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3
6
-
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1
1
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2
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1
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1
9
1
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2
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2
3
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3
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9
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1
1
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1
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1
9
1
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687988
Romand
Dynamic expression of the reti ...
Mus musculus
J. Comp. Neurol.
508
879-892
2008
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1
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9
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696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
-
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4
3
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5
-
1
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2
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3
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1
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1
1
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1
1
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1
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4
1
3
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5
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1
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3
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1
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1
1
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667934
Yamamoto
Substrate specificity analysis ...
Deinococcus radiodurans, Saccharomyces cerevisiae
Bioorg. Med. Chem.
15
1346-1355
2007
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1
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-
11
20
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2
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7
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1
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2
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24
-
2
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20
2
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2
9
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1
2
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11
9
20
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2
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1
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2
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24
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2
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20
2
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686287
Cammas
Expression of the murine retin ...
Mus musculus
Dev. Dyn.
236
2899-2908
2007
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686950
Sandell
RDH10 is essential for synthes ...
Mus musculus
Genes Dev.
21
1113-1124
2007
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1
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1
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1
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669670
Szamtari
PPARgamma controls CD1d expres ...
Homo sapiens
J. Exp. Med.
203
2351-2362
2006
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660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
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1
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2
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1
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4
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3
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1
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1
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1
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2
1
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1
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1
1
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2
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1
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4
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1
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1
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4
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1
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2
1
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660918
Miyazaki
Identification of a novel trif ...
Deinococcus radiodurans
Biochem. Biophys. Res. Commun.
336
596-602
2005
-
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1
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4
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7
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2
2
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4
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1
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1
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3
1
1
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7
1
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1
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1
1
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4
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7
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2
2
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1
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1
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3
1
1
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7
1
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