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Information on EC 2.6.1.28 - tryptophan-phenylpyruvate transaminase
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EC Tree
2.6.1.28 tryptophan-phenylpyruvate transaminaseIUBMB Comments
Valine, leucine and isoleucine can replace tryptophan as amino donor.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
aminotransferase, tryptophan-phenylpyruvate, L-tryptophan-alpha-ketoisocaproate aminotransferase, TdiD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, tryptophan-phenylpyruvate
-
-
-
-
L-tryptophan-alpha-ketoisocaproate aminotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate + L-phenylalanine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:phenylpyruvate aminotransferase
Valine, leucine and isoleucine can replace tryptophan as amino donor.
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CAS REGISTRY NUMBER
COMMENTARY
37277-87-5
-
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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
L-2-aminobutanoate + phenylpyruvate
L-phenylalanine + 2-oxobutanoate
-
-
-
-
?
L-isoleucine + phenylpyruvate
L-phenylalanine + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
-
low activity
-
-
r
L-phenylalanine + 2-oxoisohexanoate
phenylpyruvate + L-leucine
-
i.e alpha-ketoisocaproate, highest activity as amino acceptor
-
-
r
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
-
2% of the activity with alpha-ketoisocaproate
-
-
r
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
-
weak activity
-
-
r
L-tryptophan + 2-oxohexanoate
3-indole-2-oxopropanoate + L-norleucine
-
-
-
-
r
L-tryptophan + 2-oxoisohexanoate
3-indole-2-oxopropanoate + L-leucine
-
-
-
-
r
L-tryptophan + 2-oxopentanoate
3-indole-2-oxopropanoate + norvaline
-
-
-
-
r
L-tryptophan + 4-hydroxyphenylpyruvate
3-indole-2-oxopropanoate + ?
15% of the activity with phenylpyruvate
-
-
?
L-tryptophan + p-hydroxyphenylpyruvate
3-indole-2-oxopropanoate + tyrosine
-
-
-
-
r
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
2% of the activity with alpha-ketoisocaproate
-
-
r
phenylpyruvate + DL-5-hydroxytryptophan
phenylalanine + 3-(5-hydroxyindole)-2-oxopropanoate
-
-
-
-
r
phenylpyruvate + DL-histidine
phenylalanine + 3-(1H-imidazol-4-yl)-2-oxopropanoate
-
low activity
-
-
r
phenylpyruvate + L-citrulline
phenylalanine + 2-oxo-5-ureido-pentanoate
-
low activity
-
-
r
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
no activity
-
-
?
L-tryptophan + 2-oxoisopentanoate
3-indole-2-oxopropanoate + L-valine
-
i.e. L-Trp + dimethylpyruvate
-
-
r
L-tryptophan + 2-oxoisopentanoate
3-indole-2-oxopropanoate + L-valine
-
i.e. L-Trp + dimethylpyruvate
-
-
r
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
-
phenylpyruvate is the most effective amino acceptor, in the reverse reaction phenylalanine is the most effective amino donor
i.e. indolepyruvate + L-Phe
r
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
-
conversion of tryptophan into the plant indolylacetic acid
-
-
?
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
-
-
-
?
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
pyruvate, 2-oxoglutarate, and 2-oxo-(4-methylthio)butyrateare no co-substrates
for biosynthesis of terrequinone A, 3-indole-2-oxopropanoate is used for an unusual nonoxidative coupling by the tridomain nonribosomal peptide synthetase TdiA
-
?
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
-
-
i.e. indolepyruvate + L-Phe
r
phenylpyruvate + DL-isoleucine
phenylalanine + 3-methyl-2-oxopentanoate
-
-
-
-
r
phenylpyruvate + DL-isoleucine
phenylalanine + 3-methyl-2-oxopentanoate
-
-
-
-
r
phenylpyruvate + DL-leucine
phenylalanine + 4-methyl-2-oxopentanoate
-
-
-
-
r
phenylpyruvate + DL-leucine
phenylalanine + 4-methyl-2-oxopentanoate
-
-
-
-
r
phenylpyruvate + DL-methionine
phenylalanine + 4-methylsulfanyl-2-oxobutanoate
-
-
-
-
r
phenylpyruvate + DL-methionine
phenylalanine + 4-methylsulfanyl-2-oxobutanoate
-
low activity
-
-
r
phenylpyruvate + DL-valine
phenylalanine + 3-methyl-2-oxobutanoate
-
-
-
-
r
phenylpyruvate + L-tyrosine
phenylalanine + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
-
r
phenylpyruvate + L-tyrosine
phenylalanine + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
-
-
-
r
additional information
?
-
-
glutamic acid, aspartic acid, alanine, threonine, arginine, glutamine and serine are practically inactive
-
-
?
additional information
?
-
catalyzes the first enzymatic step specific to the metabolic pathway toward terrequinone A
-
-
?
additional information
?
-
no amino acceptor substrate: pyruvic acid, 2-oxoglutaric acid, 2-oxo-butyric acid, 2-oxo-valeric acid
-
-
?
additional information
?
-
-
no activity with glutamate, 2-oxoglutarate
-
-
?
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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 + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
-
conversion of tryptophan into the plant indolylacetic acid
-
-
?
additional information
?
-
catalyzes the first enzymatic step specific to the metabolic pathway toward terrequinone A
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
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
8.6 - 10.6
-
pH 8.6: about 70% of activity maximum, pH 10.6: about 80% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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). TDID_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
436
0
47705
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
expression of complete gene cluster TdiA-TdiE in Escherichia coli, in order to establish the biosynthetic pathway to terrequinone A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
5 min, without substrate or pyridoxal 5'-phosphate, complete loss of activity
additional information
-
markedly heat-stable in presence of tryptophan, phenylpyruvate or pyridoxal 5'-phosphate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of complete gene cluster TdiA-TdiE in Escherichia coli, in order to establish the biosynthetic pathway to terrequinone A
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
one-pot synthesis of di-demethylasterriquinone D from L-tryptophan and phenylpyruvic acid by use of enzymes TdiA and TdiD
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sukanya, N.K.; Vaidyanathan, C.S.
Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate
Biochem. J.
92
594-598
1964
Agrobacterium tumefaciens
brenda
Koide, Y.; Honma, M.; Shimomura, T.
L-tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas sp.
Agric. Biol. Chem.
44
2013-2019
1980
Pseudomonas sp.
-
brenda
Schneider, P.; Weber, M.; Rosenberger, K.; Hoffmeister, D.
A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones
Chem. Biol.
14
635-644
2007
Aspergillus nidulans (A7XRY8)
brenda
Balibar, C.J.; Howard-Jones, A.R.; Walsh, C.T.
Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization and bisprenylation
Nat. Chem. Biol.
3
584-592
2007
Aspergillus nidulans (A7XRY8)
brenda
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Release 2023.1 (January 2023)
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