BRENDA - Enzyme Database show
show all sequences of 1.1.1.87

Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase

Miyazaki, J.; Kobashi, N.; Nishiyama, M.; Yamane, H.; J. Biol. Chem. 278, 1864-1871 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)
Thermus thermophilus
Engineering
Amino acid exchange
Commentary
Organism
R85V
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.4
-
1-hydroxy-1,2,3-propanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
7.5
-
1-hydroxy-1,2,4-butanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
Thermus thermophilus
involved in lysine biosynthesis through alpha-aminoadipate
2-oxoadipate + CO2 + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
-
strain HB27
-
Purification (Commentary)
Commentary
Organism
-
Thermus thermophilus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
564
-
purified enzyme, pH 8.0, 60C, with 1-hydroxy-1,2,4-butanetricarboxylate as substrate
Thermus thermophilus
8579
-
purified enzyme, pH 8.0, 60C, with 1-hydroxy-1,2,3-propanetricarboxylate as substrate
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
656127
Thermus thermophilus
?
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
-
656127
Thermus thermophilus
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
involved in lysine biosynthesis through alpha-aminoadipate
656127
Thermus thermophilus
2-oxoadipate + CO2 + NADH
-
-
-
?
additional information
no activity with 3-isopropylmalate
656127
Thermus thermophilus
?
-
-
-
-
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
half life: 16.7 h
Thermus thermophilus
93.6
-
melting point
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
171
-
1-hydroxy-1,2,3-propanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
171
-
1-hydroxy-1,2,4-butanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)
Thermus thermophilus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Thermus thermophilus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
R85V
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.4
-
1-hydroxy-1,2,3-propanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
7.5
-
1-hydroxy-1,2,4-butanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
Thermus thermophilus
involved in lysine biosynthesis through alpha-aminoadipate
2-oxoadipate + CO2 + NADH
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermus thermophilus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
564
-
purified enzyme, pH 8.0, 60C, with 1-hydroxy-1,2,4-butanetricarboxylate as substrate
Thermus thermophilus
8579
-
purified enzyme, pH 8.0, 60C, with 1-hydroxy-1,2,3-propanetricarboxylate as substrate
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
656127
Thermus thermophilus
?
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
-
656127
Thermus thermophilus
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
involved in lysine biosynthesis through alpha-aminoadipate
656127
Thermus thermophilus
2-oxoadipate + CO2 + NADH
-
-
-
?
additional information
no activity with 3-isopropylmalate
656127
Thermus thermophilus
?
-
-
-
-
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
half life: 16.7 h
Thermus thermophilus
93.6
-
melting point
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
171
-
1-hydroxy-1,2,3-propanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
171
-
1-hydroxy-1,2,4-butanetricarboxylate
purified enzyme, pH 8.0, 60C
Thermus thermophilus
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
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3
4
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2
3
2
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8
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1
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6
2
1
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4
1
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1
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1
1
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3
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4
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1
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6
2
1
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4
1
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1
1
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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
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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
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-
690842
Takahashi
Characterization of key residu ...
Homo sapiens
Biochem. J.
419
113-122
2009
-
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1
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13
-
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8
1
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1
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2
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4
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1
4
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13
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8
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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-
-
-
-
-
-
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2
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4
-
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4
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2
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1
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1
2
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4
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696350
Lin
Site-directed mutagenesis as a ...
Saccharomyces cerevisiae
Biochemistry
48
7305-7312
2009
-
-
-
-
2
-
-
1
-
2
-
1
-
2
-
-
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2
-
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
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1
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2
1
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685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
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2
5
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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
5
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1
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-
4
-
3
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-
1
-
1
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-
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685539
Yamamoto
Thiahomoisocitrate: a highly p ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
16
3372-3376
2008
-
-
-
-
-
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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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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
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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
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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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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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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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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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669109
Miyazaki
Crystal structure of tetrameri ...
Thermus thermophilus
J. Bacteriol.
187
6779-6788
2005
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1
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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1
1
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1
1
1
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2
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1
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1
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3
1
1
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2
1
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656127
Miyazaki
Characterization of homoisocit ...
Thermus thermophilus
J. Biol. Chem.
278
1864-1871
2003
-
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1
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1
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2
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1
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3
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1
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2
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4
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2
2
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1
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1
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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2
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4
-
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2
2
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692332
Picozzi
Genomic organization and trans ...
Homo sapiens
FEBS Lett.
554
59-66
2003
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1
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9
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9
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692700
Wu
Cloning and characterization o ...
Bos taurus, Homo sapiens, Mus musculus
Invest. Ophthalmol. Vis. Sci.
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