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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
-
-
-
r
L-tryptophan + 2-oxoglutarate
(indol-3-yl)pyruvate + L-glutamate
-
-
-
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
(indol-3-yl)pyruvate + L-glutamate
-
-
-
-
r
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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evolution
-
related enzymes TSG1 and OsTAR1, but not OsTARL1 and OsTARL2, display marked aminotransferase activity suggesting that OsTARL1 and OsTARL2 have lost their aminotransferase activity and play other roles, with only TSG1 and OsTAR1 functioning as aminotransferases during auxin biosynthesis in rice. Possible gene redundancy in the rice tryptophan aminotransferase family. The subcellular localization is identified as the endoplasmic reticulum, while phylogenetic analysis reveals functional divergence of TSG1 and OsTAR1 from OsTARL1 and OsTARL2. TSG1 dominates the tryptophan aminotransferase family, playing a prominent role in local auxin biosynthesis in rice
metabolism
-
expression of indole-3-pyruvate decarboxylase LmIPDC2, tryptophan aminotransferase LmTAM1 and nitrilase LmNIT1 genes is mainly upregulated after adding tryptophan and correlated with IAA production, suggesting that these genes are the key components of auxin biosynthesis in Leptosphaeria maculans. Tryptamine acts as a potent inducer of IAA production, though a pathway independent of LmIPDC2/LmTAM1 may be involved. Analysis of the biosynthetic pathways in the fungus, overview
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
malfunction
-
the rice tillering and small grain 1 (tsg1) mutant, which has more tillers but a smaller panicle and grain size resulting from a reduction in endogenous auxin. TSG1 encodes a tryptophan aminotransferase that is allelic to the FISH BONE (FIB) gene. The tsg1 mutant shows hypersensitivity to indole-3-acetic acid and the competitive inhibitor of aminotransferase, L-kynurenine. TSG1 knockout results in an increased tiller number but reduction in grain number and size, and decrease in height. Deletion of the TSG1 homologues OsTAR1 (UniProt ID Q0DKE8), OsTARL1, and OsTARL2 causes no obvious changes, although the phenotype of the TSG1/OsTAR1 double mutant is intensified and infertile, suggesting gene redundancy in the rice tryptophan aminotransferase family. In line with the role of TSG1 in regulating cell development, relative expression levels of cell cycle-related genes and genes encoding expansin proteins, which affect cell expansion, are significantly downregulated in spikelets of the tsg1 mutant
physiological function
-
it is hypothesized that indole-3-acetic acid production in developing rice grains is controlled via expression of OsTAR1, OsYUC9, OsYUC11
physiological function
-
enzyme TSG1 dominates the tryptophan aminotransferase family, playing a prominent role in local auxin biosynthesis in rice, TSG1 thus affects auxin signaling and transport. Auxin is a crucial phytohormone, underlying multiple aspects of plant growth and development. TSG1 contributes to localized cell proliferation and cell expansion
physiological function
-
the enzyme influences the auxin metabolisms in the fungus and in host plants, e.g. Brassica napus
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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
Guo, T.; Chen, K.; Dong, N.Q.; Ye, W.W.; Shan, J.X.; Lin, H.X.
Tillering and small grain 1 dominates the tryptophan aminotransferase family required for local auxin biosynthesis in rice
J. Integr. Plant Biol.
62
581-600
2020
Oryza sativa Indica Group
brenda
Narukawa-Nara, M.; Nakamura, A.; Kikuzato, K.; Kakei, Y.; Sato, A.; Mitani, Y.; Yamasaki-Kokudo, Y.; Ishii, T.; Hayashi, K.; Asami, T.; Ogura, T.; Yoshida, S.; Fujioka, S.; Kamakura, T.; Kawatsu, T.; Tachikawa, M.; Soeno, K.; Shimada, Y.
Aminooxy-naphthylpropionic acid and its derivatives are inhibitors of auxin biosynthesis targeting l-tryptophan aminotransferase structure-activity relationships
Plant J.
87
245-257
2016
Arabidopsis thaliana (Q9S7N2), Arabidopsis thaliana Col-0 (Q9S7N2)
brenda
Leontovycova, H.; Trda, L.; Dobrev, P.; Sasek, V.; Gay, E.; Balesdent, M.; Burketova, L.
Auxin biosynthesis in the phytopathogenic fungus Leptosphaeria maculans is associated with enhanced transcription of indole-3-pyruvate decarboxylase LmIPDC2 and tryptophan aminotransferase LmTAM1
Res. Microbiol.
171
174-184
2020
Leptosphaeria maculans
brenda