Information on EC 2.6.1.27 - tryptophan transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.27
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RECOMMENDED NAME
GeneOntology No.
tryptophan transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate
show the reaction diagram
also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
indole-3-acetate biosynthesis II
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L-tryptophan degradation IV (via indole-3-lactate)
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L-tryptophan degradation VII (via indole-3-pyruvate)
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L-tryptophan degradation VIII (to tryptophol)
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Metabolic pathways
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Tryptophan metabolism
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tryptophan metabolism
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9022-98-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the rhizosphere of Festuca octoflora
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain 175
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Manually annotated by BRENDA team
strain 175
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain JA2
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Manually annotated by BRENDA team
strain JA2
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Manually annotated by BRENDA team
strain ATCC 12648
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Q4PDK9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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it is hypothesized that indole-3-acetic acid production in developing rice grains is controlled via expression of OsTAR1, OsYUC9, OsYUC11
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methyltryptophan + 2-oxoglutarate
3-(3-methylindole)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
can also inhibit the enzyme, stereospecific for positions 2 and 3
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-
?
5-hydroxytryptophan + 2-oxoglutarate
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
show the reaction diagram
5-hydroxytryptophan + oxaloacetate
3-(5-hydroxyindole)-2-oxopropanoate + L-aspartate
show the reaction diagram
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-
-
-
?
D-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
show the reaction diagram
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activity can be due to a different enzyme
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-
?
D-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
show the reaction diagram
DL-p-fluorophenylalanine + 2-oxoglutarate
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
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41% as effective as phenylalanine
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-
?
L-3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
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46% as effective as L-phenylalanine
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-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
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-
-
?
L-aspartate + oxaloacetate
oxaloacetate + L-aspartate
show the reaction diagram
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-
-
?
L-aspartate + phenylpyruvate
2-oxosuccinic acid + L-phenylalanine
show the reaction diagram
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10% as effective as L-glutamate
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r
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
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35% as effective as L-phenylalanine
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-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
show the reaction diagram
L-phenylalanine + 2-oxosuccinic acid
phenylpyruvate + L-aspartate
show the reaction diagram
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70% as effective as 2-oxoglutarate
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r
L-phenylalanine + oxaloacetate
phenylpyruvate + L-aspartate
show the reaction diagram
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-
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-
?
L-tryptophan + 2-oxoglutarate
(indol-3-yl)pyruvate + L-glutamate
show the reaction diagram
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
show the reaction diagram
L-tryptophan + 2-oxomethylthiobutanoate
(indol-3-yl)pyruvate + 2-aminomethylthiobutanoate
show the reaction diagram
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
show the reaction diagram
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isozymes L-TAT-1 and L-TAT-2
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-
?
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
show the reaction diagram
L-tryptophan + phenylpyruvate
(indol-3-yl)pyruvate + L-phenylalanine
show the reaction diagram
L-tyrosine + 2-oxoglutarate
L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
show the reaction diagram
L-tyrosine + oxaloacetate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-aspartate
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-tryptophan + 2-oxoglutarate
L-glutamate + 3-indole-2-oxopropanoate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Methyltryptophan
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can also act as substrate
4-Fluorophenylalanine
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32 mM, 50% inhibition
Aminooxyacetate
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L-glutamate
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inhibits activity towards tryptophan
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
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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preincubation, activates
phosphate
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maximal activity in presence of phosphate buffer, in absence reaction proceeds at 50% of that observed in optimal phosphate concentration
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.158 - 2.9
2-oxoglutarate
7
4-Fluorophenylalanine
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pH 8.0, 37C
6
L-3,4-dihydroxyphenylalanine
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pH 8.0, 37C
50
L-phenylalanine
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pH 8.0, 37C
1.22 - 15
L-tryptophan
3.8
L-tyrosine
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pH 8.0, 37C
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01152
L-kynurenine
pH and temperature not specified in the publication; pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
Aminooxyacetate
Malassezia furfur
S4UF58
pH 8.0, 42C
86
cycloserine
Malassezia furfur
S4UF58
pH 8.0, 42C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.04
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reverse reaction, purified enzyme
23.6
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partially purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
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phenylalanine
8
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assay at
8 - 9
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isozymes L-TAT-1, L-TAT-2, D-TAT
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.3
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pH 7.0: about 55% of activity maximum, pH 9.3: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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D-TAT
37
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assay at
50 - 60
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both L-TAT isozymes
55
assay at; assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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no sucess in solubilization of the enzyme from the particles
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Manually annotated by BRENDA team
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cytosol
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Manually annotated by BRENDA team
additional information
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no activity in mitochondria
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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isozyme form L-TAT-2, gel filtration
80000
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isozyme form L-TAT-1, gel filtration
97000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 10
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12 h, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low buffer concentrations: loss of activity
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unstable upon freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.40 M potassium phosphate buffer, pH 8.0, highly purified enzyme stable for at least 2 weeks
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-20C, 100fold purified enzyme, 0.4 M potassium phosphate, pH 8.0, stable for at least 9 months
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-20C, 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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0C, partially purified enzyme, stable for at least 48 h
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4C, H2O, stable for around 1 week
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
35fold
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about 900fold
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partial, 200fold
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partial, 3 isozymes: L-TAT-1 and L-TAT-2 (L-tryptophan aminotransferases), and D-TAT (D-tryptophan aminotransferase)
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partial, 3fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; expressed in Escherichia coli
expression in Escherichia coli
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 hide
LITERATURE
additional information
Q4PDK9
in isoform tam1 deletion mutant, pigment production is severely affected, and mutants produced fewer pigment compounds than the wild type