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Information on EC 2.6.1.27 - tryptophan transaminase
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2.6.1.27 tryptophan transaminaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids.
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Word Map
- 2.6.1.27
- auxin
- iaa
-
indole-3-pyruvic
- aminotransferases
- tryptamine
- indole-3-acetaldehyde
- indolepyruvate
-
gravitropism
-
tryptophan-dependent
- l-kynurenine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tryptophan aminotransferase, ostar1, l-tryptophan aminotransferase, tryptophan transaminase, vanishing tassel2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TAA1
Tam1
tryptophan aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate
also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(S)-reticuline biosynthesis I, 3-(4-hydroxyphenyl)pyruvate biosynthesis, 4-hydroxybenzoate biosynthesis I (eukaryotes), atromentin biosynthesis, indole-3-acetate biosynthesis II, indole-3-acetate biosynthesis VI (bacteria), L-phenylalanine biosynthesis I, L-phenylalanine degradation II (anaerobic), L-phenylalanine degradation III, L-phenylalanine degradation IV (mammalian, via side chain), L-phenylalanine degradation VI (reductive Stickland reaction), L-tryptophan degradation IV (via indole-3-lactate), L-tryptophan degradation VIII (to tryptophol), L-tryptophan degradation XIII (reductive Stickland reaction), L-tyrosine biosynthesis I, L-tyrosine degradation I, L-tyrosine degradation II, L-tyrosine degradation III, L-tyrosine degradation IV (to 4-methylphenol), L-tyrosine degradation V (reductive Stickland reaction), rosmarinic acid biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids.
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CAS REGISTRY NUMBER
COMMENTARY
9022-98-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyltryptophan + 2-oxoglutarate
3-(3-methylindole)-2-oxopropanoate + L-glutamate
-
can also inhibit the enzyme, stereospecific for positions 2 and 3
-
?
5-hydroxytryptophan + oxaloacetate
3-(5-hydroxyindole)-2-oxopropanoate + L-aspartate
-
-
-
?
D-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
activity can be due to a different enzyme
-
?
DL-p-fluorophenylalanine + 2-oxoglutarate
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
-
41% as effective as phenylalanine
-
?
L-3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
46% as effective as L-phenylalanine
-
?
L-aspartate + phenylpyruvate
2-oxosuccinic acid + L-phenylalanine
-
10% as effective as L-glutamate
-
r
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
35% as effective as L-phenylalanine
-
?
L-phenylalanine + 2-oxosuccinic acid
phenylpyruvate + L-aspartate
-
70% as effective as 2-oxoglutarate
-
r
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
-
isozymes L-TAT-1 and L-TAT-2
-
?
L-tyrosine + oxaloacetate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-aspartate
-
-
-
?
5-hydroxytryptophan + 2-oxoglutarate
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
-
-
-
?
5-hydroxytryptophan + 2-oxoglutarate
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
-
DL-5-hydroxytryptophan, 62% as effective as L-phenylalanine
-
?
D-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
no activity with oxaloacetate and 2-oxoglutarate as amino group acceptors
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
?
L-tryptophan + 2-oxoglutarate
(indol-3-yl)pyruvate + L-glutamate
-
-
?
L-tryptophan + 2-oxoglutarate
(indol-3-yl)pyruvate + L-glutamate
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
specific for the substrates
i.e. indole-3-pyruvate
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
role in microbial synthesis of auxins, influence on plant growth and development
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
first step in metabolic path for the conversion of L-tryptophan to indolepropionate
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
first step in metabolic path for the conversion of L-tryptophan to indolepropionate
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
initial step of biosynthetic pathway of the antibiotic indolmycin
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
52% of the activity with L-phenylalanine
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
by conversion of tryptophan into indolepyruvate, enzyme is involved in pigment biosynthesis. Additionally, substrate 2-oxo-4-methylthiobutanoate links tryptophan deamination to sulfur metabolism
L-tryptophan plus 3-indole-2-oxopropanoate may spontaneously form into indole pigments without further enzymatic activity
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
-
i.e. indole-3-pyruvate
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
2-oxoglutarate is more effective than pyruvate, oxaloacetate and glyoxylate
-
?
L-tryptophan + 2-oxomethylthiobutanoate
(indol-3-yl)pyruvate + 2-aminomethylthiobutanoate
113% of the activity of 2-oxoglutarate as amine acceptor
-
?
L-tryptophan + 2-oxomethylthiobutanoate
(indol-3-yl)pyruvate + 2-aminomethylthiobutanoate
113% of the activity of 2-oxoglutarate as amine acceptor
-
?
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
-
-
-
?
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
-
isozymes L-TAT-1 and L-TAT-2
-
?
L-tryptophan + phenylpyruvate
(indol-3-yl)pyruvate + L-phenylalanine
93% of the activity of 2-oxoglutarate as amine acceptor
-
?
L-tryptophan + phenylpyruvate
(indol-3-yl)pyruvate + L-phenylalanine
93% of the activity of 2-oxoglutarate as amine acceptor
-
?
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
?
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
49% of the activity with L-phenylalanine
-
?
additional information
?
-
TAA1 can also use Kyn as a substrate in vitro to produce kynurenic acid
-
?
additional information
?
-
TAA1 can also use Kyn as a substrate in vitro to produce kynurenic acid
-
?
additional information
?
-
-
TAA1 can also use Kyn as a substrate in vitro to produce kynurenic acid
-
?
additional information
?
-
-
TAA1 can also use Kyn as a substrate in vitro to produce kynurenic acid
-
?
additional information
?
-
no substrates: amine acceptors glyoxylic acid and hydroxypyruvate, amine donors L-phenylalanine, L-alanine, L-glycine, L-serine, L-histidine
-
?
additional information
?
-
-
no substrates: amine acceptors glyoxylic acid and hydroxypyruvate, amine donors L-phenylalanine, L-alanine, L-glycine, L-serine, L-histidine
-
?
additional information
?
-
no substrates: amine acceptors glyoxylic acid and hydroxypyruvate, amine donors L-phenylalanine, L-alanine, L-glycine, L-serine, L-histidine
-
?
additional information
?
-
-
no activity with D-phenylalanine and D-glutamic acid
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
role in microbial synthesis of auxins, influence on plant growth and development
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
first step in metabolic path for the conversion of L-tryptophan to indolepropionate
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
first step in metabolic path for the conversion of L-tryptophan to indolepropionate
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
-
initial step of biosynthetic pathway of the antibiotic indolmycin
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
by conversion of tryptophan into indolepyruvate, enzyme is involved in pigment biosynthesis. Additionally, substrate 2-oxo-4-methylthiobutanoate links tryptophan deamination to sulfur metabolism
L-tryptophan plus 3-indole-2-oxopropanoate may spontaneously form into indole pigments without further enzymatic activity
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pyridoxal 5'-phosphate
activity is highly dependent on the cofactor and increases in presence of additional cofactor
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-kynurenine
competitively inhibits TAA1/TAR activity, and Kyn treatment mimicks the loss of TAA1/TAR functions; competitively inhibits TAA1/TAR activity, and Kyn treatment mimicks the loss of TAA1/TAR functions
p-chloromercuribenzoate
-
reduced by preincubation with L-phenylalanine and pyridoxal phosphate and reversed by a subsequent preincubation with 2-mercaptoethanol
additional information
-
not affected by metal chelators and high concentration of ammonium sulfate; reduced activity in cacodylate, Tris and borate buffers
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
-
maximal activity in presence of phosphate buffer, in absence reaction proceeds at 50% of that observed in optimal phosphate concentration
additional information
-
no activation by: pyridoxine, pyridoxal, pyridoxamine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.158
2-oxoglutarate
-
cosubstrate phenylalanine , pH 8.4, 22°C approximately
2.68
L-tryptophan
-
cosubstrate tryptophan, pH 8.4, 22°C approximately
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01152
L-kynurenine
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.3
-
pH 7.0: about 55% of activity maximum, pH 9.3: about 60% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
no sucess in solubilization of the enzyme from the particles
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
it is hypothesized that indole-3-acetic acid production in developing rice grains is controlled via expression of OsTAR1, OsYUC9, OsYUC11
malfunction
-
phenotypes observed in taa mutants, including root resistance to ethylene treatment, altered shade avoidance responses, and root resistance to naphthylphthalamic acid treatments, are phenocopied by inactivating certain combinations of YUC genes. Synergistic effects between yuc and known auxin mutants are observed when TAA genes are inactivated in the known auxin mutant backgrounds. Overexpression of YUC1 in taa1/sav3 partially rescues the shade avoidance defects. Using a genetic analysis it is shown that YUC and TAA genes are in the same auxin biosynthesis pathway, with YUCs downstream of TAAs
malfunction
vt2 mutants have dramatic effects on vegetative and reproductive development. vt2 mutants share many similarities with sparse inflorescence1 (spi1) mutants in maize. both spi1 and vt2 single mutants exhibit a reduction in free auxin levels, but the spi1 vt2 double mutants do not have a further reduction compared with vt2 single mutants
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TAR1_ARATH
388
0
44064
Swiss-Prot
other Location (Reliability: 1)
TAR1_ORYSJ
441
1
47349
Swiss-Prot
other Location (Reliability: 4)
TAR2_ARATH
440
1
50007
Swiss-Prot
Secretory Pathway (Reliability: 4)
TAR2_ORYSJ
507
1
55260
Swiss-Prot
other Location (Reliability: 5)
TAA1_ARATH
391
0
44801
Swiss-Prot
other Location (Reliability: 2)
ISS1_ARATH
394
0
43762
Swiss-Prot
Mitochondrion (Reliability: 4)
A0A2C8CWY0_9GAMM
398
0
44437
TrEMBL
-
S4UF58_MALFU
476
0
52580
TrEMBL
other Location (Reliability: 3)
A0A0D1E3F3_USTMA
Ustilago maydis (strain 521 / FGSC 9021)
503
0
54711
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in isoform tam1 deletion mutant, pigment production is severely affected, and mutants produced fewer pigment compounds than the wild type
additional information
-
in isoform tam1 deletion mutant, pigment production is severely affected, and mutants produced fewer pigment compounds than the wild type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.40 M potassium phosphate buffer, pH 8.0, highly purified enzyme stable for at least 2 weeks
-
-20°C, 100fold purified enzyme, 0.4 M potassium phosphate, pH 8.0, stable for at least 9 months
-
-20°C, best stored by freezing the crude cell-free extract with 10% glycerol or by freezing the 45-60% ammonium sulfate precipitate in a phosphate buffer solution
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, 3 isozymes: L-TAT-1 and L-TAT-2 (L-tryptophan aminotransferases), and D-TAT (D-tryptophan aminotransferase)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in indole-3-acetic acid content is strongly correlated with the expression of putative IAA biosynthesis genes, OsYUC9, OsYUC11 and OsTAR1, measured by quantitative reverse transcriptase polymerase chain reaction
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Speedie, M.K.; Hornemann, U.; Floss, H.G.
Isolation and characterization of tryptophan transaminase and indolepyruvate C-methyltransferase. Enzymes involved in indolmycin biosynthesis in Streptomyces griseus
J. Biol. Chem.
250
7819-7825
1975
Streptomyces griseus
brenda
George, H.; Gabay, S.
Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase
Biochim. Biophys. Acta
167
555-566
1968
Sus scrofa
brenda
O'Neil, S.R.; DeMoss, R.D.
Tryptophan transaminase from Clostridium sporogenes
Arch. Biochem. Biophys.
127
361-369
1968
Clostridium sporogenes, Clostridium sporogenes 175
brenda
Koshiba, T.; Mito, N.; Miyakado, M.
L- And D-tryptophan aminotransferases from maize coleoptiles
J. Plant Res.
106
25-29
1993
Zea mays
-
brenda
Frankenberger, W.T.Jr.; Poth, M.
L-Tryptophan transaminase of a bacterium isolated from the rhizosphere of Festuca octoflora (Graminae)
Soil Biol. Biochem.
20
299-304
1988
Bacteria
-
brenda
Bode, R.; Birnbaum, D.
Characterization of three tryptophan aminotransferases from 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
Candida maltosa
-
brenda
Stanley, J.; Nicholas, A.; Thompson, I.; Pogson, C.
Tryptophan aminotransferase activity in rat liver
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
Rattus norvegicus
-
brenda
Lesch, T.; Bode, R.; Birnbaum, D.
Transamination of L- and D-tryptophan by a soluble and a particle-bound enzyme fraction of Rhodosporidium toruloides
Biochem. Physiol. Pflanz.
174
546-554
1979
Rhodotorula toruloides
-
brenda
Minatogawa, Y.; Noguchi, T.; Kido, R.
Purification, characteriaztion and identification of tryptophan aminotransferase from rat brain
J. Neurochem.
27
1097-1101
1976
Rattus norvegicus
brenda
Truelsen, T.A.
Indole-3-pyruvic acid as an intermediate in the conversion of tryptophan to indole-3-acetic acid. I. Characterization of tryptophan transaminase from mung bean seedlings
Physiol. Plant.
26
289-295
1972
Vigna radiata var. radiata
-
brenda
Zuther, K.; Mayser, P.; Hettwer, U.; Wu, W.; Spiteller, P.; Kindler, B.L.; Karlovsky, P.; Basse, C.W.; Schirawski, J.
The tryptophan aminotransferase Tam1 catalyses the single biosynthetic step for tryptophan-dependent pigment synthesis in Ustilago maydis
Mol. Microbiol.
68
152-172
2008
Ustilago maydis (A0A0D1E3F3), Ustilago maydis
brenda
Kumavath, R.N.; Ramana, C.V.; Sasikala, C.
L-Tryptophan catabolism by Rubrivivax benzoatilyticus JA2 occurs through indole 3-pyruvic acid pathway
Biodegradation
21
825-832
2010
Rubrivivax benzoatilyticus, Rubrivivax benzoatilyticus JA2
brenda
He, W.; Brumos, J.; Li, H.; Ji, Y.; Ke, M.; Gong, X.; Zeng, Q.; Li, W.; Zhang, X.; An, F.; Wen, X.; Li, P.; Chu, J.; Sun, X.; Yan, C.; Yan, N.; Xie, D.Y.; Raikhel, N.; Yang, Z.; Stepanova, A.N.; Alonso, J.M.; Guo, H.
A small-molecule screen identifies L-kynurenine as a competitive inhibitor of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root growth in Arabidopsis
Plant Cell
23
3944-3960
2011
Arabidopsis thaliana (Q9LR29), Arabidopsis thaliana (Q9S7N2), Arabidopsis thaliana
brenda
Phillips, K.; Skirpan, A.; Liu, X.; Christensen, A.; Slewinski, T.; Hudson, C.; Barazesh, S.; Cohen, J.; Malcomber, S.; McSteen, P.
Vanishing tassel2 encodes a grass-specific tryptophan aminotransferase required for vegetative and reproductive development in maize
Plant Cell
23
550-566
2011
Zea mays (F2FB37), Zea mays
brenda
Won, C.; Shen, X.; Mashiguchi, K.; Zheng, Z.; Dai, X.; Cheng, Y.; Kasahara, H.; Kamiya, Y.; Chory, J.; Zhao, Y.
Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis
Proc. Natl. Acad. Sci. USA
108
18518-18523
2011
Arabidopsis thaliana
brenda
Abu-Zaitoon, Y.M.; Bennett, K.; Normanly, J.; Nonhebel, H.M.
A large increase in IAA during development of rice grains correlates with the expression of tryptophan aminotransferase OsTAR1 and a grain-specific YUCCA
Physiol. Plant.
146
487-499
2012
Oryza sativa
brenda
Preuss, J.; Hort, W.; Lang, S.; Netsch, A.; Rahlfs, S.; Lochnit, G.; Jortzik, E.; Becker, K.; Mayser, P.A.
Characterization of tryptophan aminotransferase 1 of Malassezia furfur, the key enzyme in the production of indolic compounds by M.furfur
Exp. Dermatol.
22
736-741
2013
Malassezia furfur (S4UF58), Malassezia furfur, Malassezia furfur CBS 7019 (S4UF58)
brenda
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