BRENDA - Enzyme Database show
show all sequences of 2.6.1.27

Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase

George, H.; Gabay, S.; Biochim. Biophys. Acta 167, 555-566 (1968)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
preincubation, activates
Sus scrofa
additional information
no activation by: pyridoxine, pyridoxal, pyridoxamine
Sus scrofa
phosphate
maximal activity in presence of phosphate buffer, in absence reaction proceeds at 50% of that observed in optimal phosphate concentration
Sus scrofa
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-Fluorophenylalanine
32 mM, 50% inhibition
Sus scrofa
additional information
not affected by metal chelators and high concentration of ammonium sulfate; reduced activity in cacodylate, Tris and borate buffers
Sus scrofa
p-chloromercuribenzoate
reduced by preincubation with L-phenylalanine and pyridoxal phosphate and reversed by a subsequent preincubation with 2-mercaptoethanol
Sus scrofa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.74
-
2-oxoglutarate
cosubstrate phenylalanine, pH 8.0, 37C
Sus scrofa
3.8
-
L-tyrosine
pH 8.0, 37C
Sus scrofa
6
-
L-3,4-dihydroxyphenylalanine
pH 8.0, 37C
Sus scrofa
7
-
4-Fluorophenylalanine
pH 8.0, 37C
Sus scrofa
15
-
L-tryptophan
pH 8.0, 37C
Sus scrofa
50
-
L-phenylalanine
pH 8.0, 37C
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
about 900fold
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
brain
cortex
Sus scrofa
-
brain cortex
-
Sus scrofa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
7.04
-
reverse reaction, purified enzyme
Sus scrofa
Storage Stability
Storage Stability
Organism
-20C, 0.40 M potassium phosphate buffer, pH 8.0, highly purified enzyme stable for at least 2 weeks
Sus scrofa
-20C, 100fold purified enzyme, 0.4 M potassium phosphate, pH 8.0, stable for at least 9 months
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-hydroxytryptophan + 2-oxoglutarate
DL-5-hydroxytryptophan, 62% as effective as L-phenylalanine
639938
Sus scrofa
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
-
-
-
?
DL-p-fluorophenylalanine + 2-oxoglutarate
41% as effective as phenylalanine
639938
Sus scrofa
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-3,4-dihydroxyphenylalanine + 2-oxoglutarate
46% as effective as L-phenylalanine
639938
Sus scrofa
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-aspartate + phenylpyruvate
10% as effective as L-glutamate
639938
Sus scrofa
2-oxosuccinic acid + L-phenylalanine
-
-
-
r
L-histidine + 2-oxoglutarate
35% as effective as L-phenylalanine
639938
Sus scrofa
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
-
639938
Sus scrofa
L-glutamate + phenylpyruvate
-
639938
Sus scrofa
r
L-phenylalanine + 2-oxosuccinic acid
70% as effective as 2-oxoglutarate
639938
Sus scrofa
phenylpyruvate + L-aspartate
-
-
-
r
L-tryptophan + 2-oxoglutarate
52% of the activity with L-phenylalanine
639938
Sus scrofa
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
49% of the activity with L-phenylalanine
639938
Sus scrofa
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
additional information
substrate specificity
639938
Sus scrofa
?
-
-
-
-
additional information
no activity with D-phenylalanine and D-glutamic acid
639938
Sus scrofa
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Sus scrofa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
phenylalanine
Sus scrofa
8
-
assay at
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate
Sus scrofa
pyridoxamine 5'-phosphate
pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate
Sus scrofa
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
preincubation, activates
Sus scrofa
additional information
no activation by: pyridoxine, pyridoxal, pyridoxamine
Sus scrofa
phosphate
maximal activity in presence of phosphate buffer, in absence reaction proceeds at 50% of that observed in optimal phosphate concentration
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate
Sus scrofa
pyridoxamine 5'-phosphate
pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate
Sus scrofa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-Fluorophenylalanine
32 mM, 50% inhibition
Sus scrofa
additional information
not affected by metal chelators and high concentration of ammonium sulfate; reduced activity in cacodylate, Tris and borate buffers
Sus scrofa
p-chloromercuribenzoate
reduced by preincubation with L-phenylalanine and pyridoxal phosphate and reversed by a subsequent preincubation with 2-mercaptoethanol
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.74
-
2-oxoglutarate
cosubstrate phenylalanine, pH 8.0, 37C
Sus scrofa
3.8
-
L-tyrosine
pH 8.0, 37C
Sus scrofa
6
-
L-3,4-dihydroxyphenylalanine
pH 8.0, 37C
Sus scrofa
7
-
4-Fluorophenylalanine
pH 8.0, 37C
Sus scrofa
15
-
L-tryptophan
pH 8.0, 37C
Sus scrofa
50
-
L-phenylalanine
pH 8.0, 37C
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
about 900fold
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
brain
cortex
Sus scrofa
-
brain cortex
-
Sus scrofa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
7.04
-
reverse reaction, purified enzyme
Sus scrofa
Storage Stability (protein specific)
Storage Stability
Organism
-20C, 0.40 M potassium phosphate buffer, pH 8.0, highly purified enzyme stable for at least 2 weeks
Sus scrofa
-20C, 100fold purified enzyme, 0.4 M potassium phosphate, pH 8.0, stable for at least 9 months
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-hydroxytryptophan + 2-oxoglutarate
DL-5-hydroxytryptophan, 62% as effective as L-phenylalanine
639938
Sus scrofa
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
-
-
-
?
DL-p-fluorophenylalanine + 2-oxoglutarate
41% as effective as phenylalanine
639938
Sus scrofa
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-3,4-dihydroxyphenylalanine + 2-oxoglutarate
46% as effective as L-phenylalanine
639938
Sus scrofa
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-aspartate + phenylpyruvate
10% as effective as L-glutamate
639938
Sus scrofa
2-oxosuccinic acid + L-phenylalanine
-
-
-
r
L-histidine + 2-oxoglutarate
35% as effective as L-phenylalanine
639938
Sus scrofa
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
-
639938
Sus scrofa
L-glutamate + phenylpyruvate
-
639938
Sus scrofa
r
L-phenylalanine + 2-oxosuccinic acid
70% as effective as 2-oxoglutarate
639938
Sus scrofa
phenylpyruvate + L-aspartate
-
-
-
r
L-tryptophan + 2-oxoglutarate
52% of the activity with L-phenylalanine
639938
Sus scrofa
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
49% of the activity with L-phenylalanine
639938
Sus scrofa
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
additional information
substrate specificity
639938
Sus scrofa
?
-
-
-
-
additional information
no activity with D-phenylalanine and D-glutamic acid
639938
Sus scrofa
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Sus scrofa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
phenylalanine
Sus scrofa
8
-
assay at
Sus scrofa
Other publictions for EC 2.6.1.27
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)
738172
Preuss
Characterization of tryptophan ...
Malassezia furfur, Malassezia furfur CBS 7019
Exp. Dermatol.
22
736-741
2013
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1
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2
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1
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1
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723349
Abu-Zaitoon
A large increase in IAA during ...
Oryza sativa
Physiol. Plant.
146
487-499
2012
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4
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720687
He
A small-molecule screen identi ...
Arabidopsis thaliana
Plant Cell
23
3944-3960
2011
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4
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720689
Phillips
Vanishing tassel2 encodes a gr ...
Zea mays
Plant Cell
23
550-566
2011
-
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3
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1
1
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720922
Won
Conversion of tryptophan to in ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
108
18518-18523
2011
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1
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1
1
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702493
Kumavath
L-Tryptophan catabolism by Rub ...
Rubrivivax benzoatilyticus, Rubrivivax benzoatilyticus JA2
Biodegradation
21
825-832
2010
-
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6
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2
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1
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2
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689054
Zuther
The tryptophan aminotransferas ...
Ustilago maydis
Mol. Microbiol.
68
152-172
2008
-
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-
-
1
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1
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4
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1
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1
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639941
Koshiba
-
L- And D-tryptophan aminotrans ...
Zea mays
J. Plant Res.
106
25-29
1993
-
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3
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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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3
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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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-
-
-
-
639942
Frankenberger
-
L-Tryptophan transaminase of a ...
Bacteria
Soil Biol. Biochem.
20
299-304
1988
-
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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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639943
Bode
-
Characterization of three tryp ...
Candida maltosa
Prog. Tryptophan Serotonin Res. Proc. -Meet. Int. Study Group Tryptophan Res. ISTRY (Schlossberger, H. G. , ed. ) 4th, Meeting Date1983, de Gruyter
Berlin
769-772
1984
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2
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639944
Stanley
-
Tryptophan aminotransferase ac ...
Rattus norvegicus
Prog. Tryptophan Serotonin Res. , Proc. -Meet. Int. Study Group Tryptophan Res. ISTRY (Schlossberger, H. G. , ed. ) 4th, Meeting Date1983, de Gruyter
Berlin
665-668
1984
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1
1
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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639945
Lesch
-
Transamination of L- and D-try ...
Rhodotorula toruloides
Biochem. Physiol. Pflanz.
174
546-554
1979
1
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1
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2
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639946
Minatogawa
Purification, characteriaztion ...
Rattus norvegicus
J. Neurochem.
27
1097-1101
1976
-
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1
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3
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1
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2
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1
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2
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10
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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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2
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10
-
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1
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1
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-
441312
Speedie
Isolation and characterization ...
Streptomyces griseus
J. Biol. Chem.
250
7819-7825
1975
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2
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6
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1
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1
6
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1
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-
639947
Truelsen
-
Indole-3-pyruvic acid as an in ...
Vigna radiata var. radiata
Physiol. Plant.
26
289-295
1972
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639938
George
Brain aromatic aminotransferas ...
Sus scrofa
Biochim. Biophys. Acta
167
555-566
1968
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639939
O'Neil
Tryptophan transaminase from C ...
Clostridium sporogenes 175, Clostridium sporogenes
Arch. Biochem. Biophys.
127
361-369
1968
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