BRENDA - Enzyme Database
show all sequences of 2.6.1.39

Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase

Bulfer, S.L.; Brunzelle, J.S.; Trievel, R.C.; Protein Sci. 22, 1417-1424 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Crystallization (Commentary)
Crystallization
Organism
to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P53090
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8
Saccharomyces cerevisiae
Other publictions for EC 2.6.1.39
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)
737334
Rzad
Characterization of two aminot ...
Candida albicans, Candida albicans ATCC MYA-2876
Acta Biochim. Pol.
62
903-912
2015
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1
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2
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4
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2
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3
1
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1
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1
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2
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4
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3
1
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1
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739600
Bulfer
Crystal structure of Saccharom ...
Saccharomyces cerevisiae
Protein Sci.
22
1417-1424
2013
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1
1
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5
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721430
Karsten
Mechanism of the aromatic amin ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
516
67-74
2011
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1
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6
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1
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1
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1
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5
1
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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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6
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1
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1
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5
1
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4
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1
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703133
Han
Structure, expression, and fun ...
Homo sapiens, Mus musculus, Rattus norvegicus
Cell. Mol. Life Sci.
67
353-368
2010
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1
-
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1
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1
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3
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1
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4
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1
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3
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4
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1
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3
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721926
Han
Thermal stability, pH dependen ...
Mus musculus
BMC Biochem.
11
0019
2010
-
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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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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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1
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1
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1
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702069
Ouchi
Dual roles of a conserved pair ...
Thermus thermophilus
Biochem. Biophys. Res. Commun.
388
21-27
2009
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-
1
1
3
-
-
24
-
-
-
-
-
2
-
-
1
-
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-
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4
-
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12
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1
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1
1
1
3
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24
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1
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4
-
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12
-
-
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-
-
24
24
689965
Tomita
Mechanism for multiple-substra ...
Thermus thermophilus
Proteins
75
348-359
2008
-
-
-
1
-
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-
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2
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5
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1
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1
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5
-
-
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1
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-
702779
Han
Substrate specificity and stru ...
Homo sapiens
Biosci. Rep.
28
205-215
2008
-
-
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-
-
-
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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
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659885
Miyazaki
alpha-Aminoadipate aminotransf ...
Thermus thermophilus
Microbiology
150
2327-2334
2004
-
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1
-
1
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4
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3
-
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4
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7
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7
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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3
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7
-
7
1
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-
4
-
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-
639985
Goh
Characterization of the human ...
Homo sapiens
Mol. Genet. Metab.
76
172-180
2002
-
1
1
-
-
-
-
-
-
-
1
1
-
7
-
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-
-
8
-
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2
-
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-
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-
1
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1
2
1
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1
1
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8
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2
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636625
Buchli
Cloning and functional express ...
Rattus norvegicus
J. Biol. Chem.
270
29330-29335
1995
-
1
1
-
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-
-
-
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3
1
-
2
-
-
1
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-
1
1
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4
1
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1
1
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3
1
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1
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1
1
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4
1
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-
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-
639983
Okuno
2-Aminoadipate-2-oxoglutarate ...
Homo sapiens
Enzyme Protein
47
136-148
1993
-
-
-
-
-
-
-
8
3
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3
1
-
2
-
-
1
-
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3
2
-
5
1
-
-
-
-
2
-
1
-
-
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-
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8
3
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3
1
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1
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3
2
-
5
1
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-
-
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2
-
1
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636621
Mawal
-
Purification and properties of ...
Rattus norvegicus
Biochem. J.
279
595-599
1991
-
-
-
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1
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1
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1
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1
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3
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1
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1
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1
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3
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-
-
-
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636622
Mawal
alpha-Aminoadipate and kynuren ...
Rattus norvegicus
J. Biol. Chem.
266
2573-2575
1991
-
-
-
-
-
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-
1
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3
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1
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3
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1
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1
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1
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3
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1
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639981
Mawal
Purification and properties of ...
Rattus norvegicus
Prep. Biochem.
21
63-73
1991
-
-
-
-
-
-
-
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2
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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
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1
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-
-
-
639979
Deshmukh
Purification and properties of ...
Bos taurus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Biochem. J.
261
761-768
1989
-
-
-
-
-
1
19
4
4
-
2
2
-
165
-
-
2
-
-
4
1
2
26
2
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
1
-
19
-
4
4
-
2
2
-
-
-
2
-
4
1
2
26
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
636620
Hartline
Kynurenine aminotransferase fr ...
Rattus norvegicus
Methods Enzymol.
113
664-672
1985
-
-
-
-
-
-
-
-
1
-
2
1
-
1
-
-
1
-
-
1
2
-
6
1
-
-
-
-
-
-
1
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-
-
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-
-
-
-
-
-
-
-
-
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-
1
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2
1
-
-
-
1
-
1
2
-
6
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
636623
Takeuchi
Purification, characterization ...
Rattus norvegicus, Rattus norvegicus Wistar
Biochim. Biophys. Acta
743
323-330
1983
-
-
-
-
-
-
1
1
2
-
1
-
-
167
-
-
1
-
-
2
2
1
1
1
-
-
1
-
1
-
-
-
-
-
-
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-
-
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-
-
-
-
1
-
1
2
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1
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1
-
2
2
1
1
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
639976
Tobes
alpha-Aminoadipate aminotransf ...
Rattus norvegicus
J. Biol. Chem.
252
4591-4599
1977
-
-
-
-
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-
1
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-
3
1
-
2
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-
1
-
-
2
2
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3
1
-
-
1
-
-
-
-
1
-
-
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-
-
-
1
-
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-
1
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-
-
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3
1
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-
1
-
2
2
-
3
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
639975
Tobes
L-kynurenine aminotransferase ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
62
390-397
1975
-
-
-
-
-
-
1
-
-
-
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1
-
1
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1
-
-
2
-
1
3
-
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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
3
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-
639974
Matsuda
Separation and specificity of ...
Saccharomyces cerevisiae
J. Biol. Chem.
244
3352-3358
1969
-
-
-
-
-
-
-
-
2
-
2
1
-
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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1
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2
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2
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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