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Enzyme Nomenclature
Information on EC 2.6.1.27 - tryptophan transaminase
for references in articles please use BRENDA:EC2.6.1.27
Word Map on EC 2.6.1.27
- 2.6.1.27
- auxin
-
indole-3-pyruvic
-
indole-3-acetic
- iaa
-
yucca
- indolepyruvate
-
aminotransferases
-
gravitropism
- tryptamine
- indole-3-acetaldehyde
-
tryptophan-dependent
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.6.1.27
-
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RECOMMENDED NAME
GeneOntology No.
tryptophan transaminase
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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
amino group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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
-
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
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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
Q4PDK9
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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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
Q4PDK9
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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INHIBITORS
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
-
high salt concentrations activate; 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; 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
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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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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
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
expressed in Escherichia coli; expressed in Escherichia coli
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Q4PDK9
in isoform tam1 deletion mutant, pigment production is severely affected, and mutants produced fewer pigment compounds than the wild type
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.27)
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