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3-methyltryptophan + 2-oxoglutarate
3-(3-methylindole)-2-oxopropanoate + L-glutamate
-
can also inhibit the enzyme, stereospecific for positions 2 and 3
-
?
5-hydroxytryptophan + 2-oxoglutarate
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
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
-
?
D-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
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 + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + oxaloacetate
oxaloacetate + L-aspartate
-
-
-
?
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-oxoglutarate
L-glutamate + phenylpyruvate
L-phenylalanine + 2-oxosuccinic acid
phenylpyruvate + L-aspartate
-
70% as effective as 2-oxoglutarate
-
r
L-phenylalanine + oxaloacetate
phenylpyruvate + L-aspartate
-
-
-
?
L-tryptophan + 2-oxoglutarate
(indol-3-yl)pyruvate + L-glutamate
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
L-tryptophan + 2-oxomethylthiobutanoate
(indol-3-yl)pyruvate + 2-aminomethylthiobutanoate
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
-
isozymes L-TAT-1 and L-TAT-2
-
?
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
L-tryptophan + phenylpyruvate
(indol-3-yl)pyruvate + L-phenylalanine
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
L-tyrosine + oxaloacetate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-aspartate
-
-
-
?
additional information
?
-
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
-
?
D-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
D-TAT
-
?
L-phenylalanine + 2-oxoglutarate

L-glutamate + phenylpyruvate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
-
-
-
r
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
?
-
-
substrate specificity
-
?
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-tryptophan
-
?
additional information
?
-
-
substrate specificity
-
?
additional information
?
-
-
no activity with D-phenylalanine and D-glutamic acid
-
?
additional information
?
-
-
substrate specificity
-
?
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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