Information on EC 2.6.1.57 - aromatic-amino-acid transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.57
-
RECOMMENDED NAME
GeneOntology No.
aromatic-amino-acid transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S)-reticuline biosynthesis I
-
-
4-hydroxybenzoate biosynthesis I (eukaryotes)
-
-
4-hydroxyphenylpyruvate biosynthesis
-
-
atromentin biosynthesis
-
-
L-phenylalanine biosynthesis I
-
-
L-phenylalanine biosynthesis III (cytosolic, plants)
-
-
L-phenylalanine degradation II (anaerobic)
-
-
L-phenylalanine degradation III
-
-
L-tyrosine biosynthesis I
-
-
L-tyrosine degradation I
-
-
L-tyrosine degradation II
-
-
L-tyrosine degradation III
-
-
L-tyrosine degradation IV (to 4-methylphenol)
-
-
rosmarinic acid biosynthesis I
-
-
methionine metabolism
-
-
phenylalanine metabolism
-
-
Cysteine and methionine metabolism
-
-
Lysine biosynthesis
-
-
Tyrosine metabolism
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Novobiocin biosynthesis
-
-
Isoquinoline alkaloid biosynthesis
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
aromatic-amino-acid:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. L-Methionine can also act as donor, but more slowly; oxaloacetate can act as acceptor. Controlled proteolysis converts the enzyme into EC 2.6.1.1 aspartate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
37332-38-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain T30
-
-
Manually annotated by BRENDA team
strain T30
-
-
Manually annotated by BRENDA team
gramicidin S-producing
-
-
Manually annotated by BRENDA team
isoenzymes AT-I and AT-II
-
-
Manually annotated by BRENDA team
strain 47
-
-
Manually annotated by BRENDA team
strain 47
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoenzymes AT-I and AT-II
-
-
Manually annotated by BRENDA team
aromatic aminotransferase I
-
-
Manually annotated by BRENDA team
strains CB 60 and CB 6
-
-
Manually annotated by BRENDA team
and other Gluconacetobacter strains, 1 isoform
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
aromatic aminotransferase AT-1; aromatic aminotransferase AT-2
-
-
Manually annotated by BRENDA team
strain A15, 3 isoforms
-
-
Manually annotated by BRENDA team
strain A15, 3 isoforms
-
-
Manually annotated by BRENDA team
biovar trifolii
-
-
Manually annotated by BRENDA team
aromatic aminotransferases I and II
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dioxo-4-phenylbutyric acid + L-Asp
(2S)-2-amino-4-oxo-4-phenylbutyric acid + oxaloacetate
show the reaction diagram
2-amino-3-phenylpropanol + 2-oxoglutarate
2-oxo-3-phenylpropanol + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 6
-
?
2-oxo-4-phenylbut-3-enoic acid + L-Asp
(3E,2S)-2-amino-4-phenylbutenoic acid + oxaloacetate
show the reaction diagram
2-oxo-4-phenylbutyrate + L-Asp
2-amino-4-phenylbutyrate + oxaloacetate
show the reaction diagram
2-oxo-4-phenylbutyrate + L-Glu
2-amino-4-phenylbutyrate + 2-oxoglutarate
show the reaction diagram
2-oxo-4-phenylbutyrate + L-Phe
2-amino-4-phenylbutyrate + phenylpyruvate
show the reaction diagram
2-oxo-4-phenylbutyric acid + L-aspartate
L-homophenylalanine + oxaloacetate
show the reaction diagram
2-oxoglutarate + Asp
L-glutamate + 2-oxosuccinic acid
show the reaction diagram
2-oxoglutarate + Glu
Glu + 2-oxoglutarate
show the reaction diagram
2-oxoglutarate + Phe
L-glutamate + phenylpyruvate
show the reaction diagram
2-oxoglutarate + Tyr
L-glutamate + 4-hydroxyphenylpyruvate
show the reaction diagram
3-iodo-L-tyrosine + 2-oxoglutarate
3-(3-iodophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
3-iodo-L-tyrosine + oxaloacetate
3-(3-iodophenyl)-2-oxopropanoate + L-aspartate
show the reaction diagram
-
-
-
?
4-hydroxyphenylpyruvate + Asp
Tyr + 2-oxosuccinate
show the reaction diagram
4-hydroxyphenylpyruvate + Glu
Tyr + 2-oxoglutarate
show the reaction diagram
4-hydroxyphenylpyruvate + L-tryptophan
L-tyrosine + 3-indole-2-oxopropanoate
show the reaction diagram
4-hydroxyphenylpyruvate + Phe
tyr + phenylpyruvate
show the reaction diagram
4-hydroxyphenylpyruvate + Tyr
Tyr + 4-hydroxyphenylpyruvate
show the reaction diagram
5-hydroxytryptophan + 2-oxoglutarate
3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
19.5% of the activity with phenylalanine
-
?
alpha-ketomethiobutyrate + L-glutamine
2-oxoglutaramide + L-methionine
show the reaction diagram
alpha-ketomethiobutyrate + L-phenylalanine
L-methionine + phenylpyruvate
show the reaction diagram
alpha-ketomethiobutyrate + L-tryptophan
L-methionine + indolepyruvate
show the reaction diagram
alpha-ketomethiobutyrate + L-tyrosine
L-methionine + hydroxyphenylpyruvate
show the reaction diagram
alpha-ketomethiobutyrate + phenylalanine
methionine + phenylpyruvate
show the reaction diagram
alpha-ketomethiobutyrate + tryptophan
methionine + indolepyruvate
show the reaction diagram
alpha-ketomethiobutyrate + tyrosine
methionine + hydroxyphenylpyruvate
show the reaction diagram
arginine + alpha-ketomethiobutyrate
? + methionine
show the reaction diagram
-
-
-
?
aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
aspartate + 3-phenylpyruvate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
-
r
diphenylpyruvate + L-phenylalanine
L-diphenylalanine + phenylpyruvate
show the reaction diagram
L-5-fluorotryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-5-methyltryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + alpha-ketomethiobutyrate
pyruvate + L-methionine
show the reaction diagram
L-arogenate + indolepyruvate
L-tryptophan + 3-(1-carboxy-4-hydroxycyclohexa-2,5-dienyl)2-oxopropanoate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
r
L-aspartate + 3-(4-hydroxyphenyl)pyruvate
L-tyrosine + oxaloacetate
show the reaction diagram
-
-
r
L-aspartate + alpha-ketomethiobutyrate
oxaloacetate + L-methionine
show the reaction diagram
L-cysteine + alpha-ketomethiobutyrate
2-oxo-3-thiopropanoate + L-methionine
show the reaction diagram
L-glutamate + 2-oxo-4-phenylbutyrate
L-homophenylalanine + 2-oxoglutarate
show the reaction diagram
L-glutamate + phenylglyoxylate
L-phenylglycine + 2-oxoglutarate
show the reaction diagram
L-glutamine + indole pyruvate
2-oxoglutamine + L-tryptophan
show the reaction diagram
-
AAT I and II
-
?
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
L-histidine + alpha-ketomethiobutyrate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-methionine
show the reaction diagram
-
-
-
?
L-histidine + indole pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-tryptophan
show the reaction diagram
-
-
-
?
L-isoleucine + alpha-ketomethiobutyrate
3-methyl-2-oxo-pentanoate + L-methionine
show the reaction diagram
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + indole pyruvate
4-methyl-2-oxopentanoate + L-tryptophan
show the reaction diagram
-
-
-
?
L-lysine + alpha-ketomethiobutyrate
2-oxo-6-amino-hexanoate + L-methionine
show the reaction diagram
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-methionine + indole pyruvate
4-methylsulfanyl-2-oxobutanoate + L-tryptophan
show the reaction diagram
-
AAT I and II
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-phenylalanine + oxaloacetate
phenylpyruvate + ?
show the reaction diagram
-
-
-
?
L-phenylalanine + oxaloacetate
phenylpyruvate + L-aspartate
show the reaction diagram
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
-
2.1% of the activity with 2-oxoglutarate
-
?
L-phenylalanine methylester + 2-oxoglutarate
2-oxo-3-phenylpropanoate methylester + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 6
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
L-tryptophan + indole pyruvate
3-indole-2-oxopropanoate + L-tryptophan
show the reaction diagram
-
-
-
?
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
show the reaction diagram
L-tryptophan + phenylpyruvate
3-indole-2-oxopropanoate + L-phenylalanine
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
at about 25% of the rate with L-phenylalanine
-
-
-
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
L-tyrosine + indole pyruvate
4-hydroxyphenylpyruvate + L-tryptophan
show the reaction diagram
-
-
-
?
L-valine + alpha-ketomethiobutyrate
3-methyl-2-oxo-butanoate + L-methionine
show the reaction diagram
-
-
-
?
oxaloacetate + Asp
Asp + oxaloacetate
show the reaction diagram
oxaloacetate + Glu
Asp + 2-oxoglutarate
show the reaction diagram
oxaloacetate + Phe
Asp + phenylpyruvate
show the reaction diagram
oxaloacetate + Tyr
Asp + 4-hydroxyphenylpyruvate
show the reaction diagram
p-aminophenylalanine + 2-oxoglutarate
p-aminophenylpyruvate + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 60 and CB 6
-
?
p-aminophenylserine + 2-oxoglutarate
3-hydroxy-2-oxo-3-(p-aminophenyl)propanoic acid + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 60 and CB 6
-
?
p-aminophenylserinol + 2-oxoglutarate
3-(p-aminophenyl)-1,3-propanediol + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 60 and CB 6
-
?
p-nitrophenylserine + 2-oxoglutarate
3-hydroxy-2-oxo-3-(p-nitrophenyl)propanoic acid + L-glutamate
show the reaction diagram
-
aromatic aminotransferase from strain CB 60 and CB 6
-
?
phenylpyruvate + Asp
Phe + 2-oxosuccinate
show the reaction diagram
phenylpyruvate + Glu
Phe + 2-oxoglutarate
show the reaction diagram
phenylpyruvate + Phe
Phe + phenylpyruvate
show the reaction diagram
phenylpyruvate + Tyr
Phe + 3-(4-hydroxyphenyl)-2-oxopropanoic acid
show the reaction diagram
prephenate + Asp
arogenate + 2-oxosuccinate
show the reaction diagram
prephenate + Glu
arogenate + 2-oxoglutarate
show the reaction diagram
prephenate + L-glutamate
1-carboxy-4-hydroxy-2,5-cyclohexadien-1-alanine + 2-oxoglutarate
show the reaction diagram
prephenate + L-tryptophan
1-carboxy-4-hydroxy-2,5-cyclohexadien-1-alanine + 3-indole-2-oxopropanoate
show the reaction diagram
-
-
-
?
prephenate + Phe
arogenate + phenylpyruvate
show the reaction diagram
prephenate + Tyr
arogenate + 4-hydroxyphenylpyruvate
show the reaction diagram
additional information
?
-
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
alpha-ketomethiobutyrate + phenylalanine
methionine + phenylpyruvate
show the reaction diagram
alpha-ketomethiobutyrate + tryptophan
methionine + indolepyruvate
show the reaction diagram
alpha-ketomethiobutyrate + tyrosine
methionine + hydroxyphenylpyruvate
show the reaction diagram
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
additional information
-
addition of pyridoxal 5'-phosphate increases the activity of the purified enzyme only slightly
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-trichlorophenoxyacetic acid
-
-
3-(2-hydroxyphenyl)propionic acid
-
-
3-(2-methoxyphenyl)propionic acid
-
-
3-(3,4,5-trimethoxyphenyl)propionic acid
-
-
3-(3,4-dimethoxyphenyl)propionic acid
-
-
3-(3-methoxyphenyl)propionic acid
-
-
3-(4-hydroxyphenyl)propionic acid
-
-
3-(4-methoxyphenyl)propionic acid
-
-
3-(p-tolyl)propionic acid
-
-
3-cyclohexylpropionic acid
-
-
3-cyclopentylpropionic acid
-
-
3-indoleacetic acid
-
-
3-indolebutyric acid
-
-
3-indolepropionic acid
-
-
3-Phenylpropionic acid
-
-
4-(2-thienyl)butyric acid
-
-
4-(4-nitrophenyl)butyric acid
-
-
4-aminohydrocinnamic acid
-
-
4-cyclohexylbutyric acid
-
-
4-hydroxyphenylpyruvate
-
substrate inhibition
4-Phenylbutyric acid
-
-
5-phenylvaleric acid
-
-
Aminooxyacetate
-
-
carbidopa
inhibitor of pyridoxal phosphate-dependent enzymes. almost complete inhibition at 0.5 mM
cycloserine
-
0.15 mM, 89% inhibition of aromatic aminotransferase from strain CB 6
Indole pyruvate
-
substrate inhibition
indole-3-pyruvic acid
-
competitive inhibition
Isonicotinohydrazide
-
36% inhibition of aromatic aminotransferase from strain CB 60, enzyme from strain CB 6 is not inhibited
L-cysteine
-
10 mM
methionine
-
10 mM, inhibits activity of isoenzyme ArAT-I with 1 mM tyrosine by 23%, isoenzyme ArAT-II is not affected
phenylhydrazine
phenylpyruvate
-
substrate inhibition
prephenate
-
substrate inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2-oxo-4-methylpentanoate
-
pH 7.6, 37C
0.14 - 38
2-oxoglutarate
0.059
3-(4-hydroxyphenyl)pyruvate
-
pH 8.0, 25C, cosubstrate aspartate
0.032 - 0.05
4-hydroxyphenylpyruvate
0.33
alpha-ketomethiobutyrate
0.8
hydroxyphenylpyruvate
-
-
0.06 - 0.1
Indolepyruvate
0.36
L-5-fluorotryptophan
-
-
1.2
L-5-methyltryptophan
-
-
0.45
L-arogenate
-
pH 8.6, 37C, AAT I
1.8 - 8.4
L-aspartate
0.28
L-glutamate
-
pH 7.6, 37C
7
L-glutamine
-
pH 8.6, 37C, AAT I
0.35 - 70
L-histidine
4 - 7.1
L-leucine
1.5 - 5
L-methionine
0.06 - 16.6
L-phenylalanine
0.095 - 16.6
L-tryptophan
0.042 - 15
L-tyrosine
0.12 - 5.1
oxaloacetate
2.18
phenylalanine
0.02 - 0.083
phenylpyruvate
0.08
prephenate
-
pH 8.6, 37C, AAT I
0.001 - 0.025
pyridoxal 5'-phosphate
8.8
pyruvate
-
pH 8.0
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
225 - 278
2-oxoglutarate
140 - 290
L-aspartate
152 - 1200
L-phenylalanine
62 - 350
L-tryptophan
72 - 500
L-tyrosine
500
oxaloacetate
Escherichia coli
-
pH 7.3, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 10
4-hydroxyphenylpyruvate
0.17
indole-3-pyruvic acid
-
-
0.3 - 1.5
indolpyruvate
0.5 - 15
phenylpyruvate
0.4 - 15
prephenate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.49
-
strain CB 6
1.59
-
strain CB 60
1.8
-
with tyrosine
2.96
-
with aspartate
3.8
-
with tryptophan
6.5
-
with phenylalanine
110
-
isoenzyme ArAT-I
424
-
isoenzyme ArAT-II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
L-glutamate, aromatic aminotransferase AT-1
7
-
L-Phe, L-Tyr, L-Asp or L-Glu as substrate, aromatic aminotransferase AT-2
7.2 - 7.6
-
phenylalanine
7.8 - 9
-
strain CB 6
8.4 - 9
-
strain CB 60
8.4
-
L-Phe or L-Tyr, aromatic aminotransferase AT-1
8.5
-
with L-tryptophan and its derivatives as substrates
8.5 - 9
-
phenylalanine
8.7
-
tryptophan
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
50% of maximal activity at pH 6.0 and pH 9.5
6 - 9.6
-
approx. 50% of maximal activity at pH 6.0 and pH 9.6
6 - 10
-
approx. 25% of maximal activity at pH 10.0, tryptophan; approx. 40% of maximal activity at pH 6.0, tryptophan
6 - 9.5
-
approx. 45% of maximal activity at pH 6.0,: approx. 60% of maximal activity at pH 9.5, phenylalanine
6 - 10
-
approx. 50% of maximal activity at pH 6.0; approx. 60% of maximal activity at pH 10.0
6.5 - 10
-
approx. 45% of maximal activity at pH 6.5, approx. 50% of maximal activity at pH 10
7 - 9.5
-
approx. 30% of maximal activity at pH 7.0 and pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
at pH 8.5
40
-
strain CB 60
57.5
-
strain CB 6
additional information
-
temperature optimum seems to be above 95C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 95
-
extremely thermostable aromatic aminotransferase from hyperthermophilic archaeon, very low activity at 30C, approx. 50% of maximal activity at 65C
30 - 105
-
virtually inactive at 30C, approx. 50% of maximal ArAT-I activity at 70C, approx. 50% of ArAT-II activity at 80C, isoenzymes ArAT-I and II
37 - 80
-
37C: about 35% of maximal activity, 50C: about 90% of maximal activity, 80C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
-
gel filtration
55000 - 59000
-
-
56000
-
recombinant enzyme, gel filtration
63500
-
gel filtration
66000
-
gel filtration
71000
-
gel filtration
84000
-
homodimeric form, gel filtration
85000
-
isoenzyme AAT-II, gel filtration
100000
-
gel filtration, sucrose density gradient centrifugation
105000
-
isoenzyme AAT-III, gel filtration
110000
-
isoenzyme ArAT-I, gel filtration
120000
-
enzymes from strain CB 60 and CB 6, gel filtration
126000
-
gel filtration
150000
-
ArAT-I, gel filtration
152000
-
AT-I, gel filtration
160000
-
AT-I, gel filtration
170000
-
tetrameric form, gel filtration
260000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 44000, SDS-PAGE
tetramer
-
4 * 42000, tetrameric enzyme form, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of unliganded pdAroAT, pdAroAT in a complex with maleate and 3-phenylpropionate at 2.33 A, 2.5 A and 2.3 A resolution
-
tertiary structures of pdAroAT complexed with nine kind of inhibitors: 3-indolebutyric acid, 4-phenylbutyric acid, 5-phenylvaleric acid, 4-(2-thienyl)butyric acid, cyclohexanepropionic acid, 4-amminohydrocinnamic acid, 3-(p-tolyl)-propionic acid and 3-(3,4-dimethoxyphenyl)propionic acid, crystals of the maleate complex of pdAroAT are made by the micro-seeding method using 24% poly(ethylene)glycol 4000, 200 mM sodium maleate, pH 5.7 and 5 mM MgCl2 as precipitating buffer, cocrystallized inhibitor maleate is replaced by soaking the crystals in 24% poly(ethylene)glycol 4000, 100 mM sodium citrate, pH 5.7 containing 100 mM inhibitor for 10 h
-
hanging drop vapor diffusion, an equi-volume of 3 M 1,6-hexanediol solution at pH 7.5, 100 mM HEPES buffer, containing 10 mM MgCl2 is added to a protein solution containing 1.6% AeATPh and 0.02 mM pyridoxal 5'-phosphate, a droplet of the solution is equilibrated with 1 ml of 3 M 1,6-hexane-di-ol solution, crystals are grown at room temperature for 1 week, crystal structure of the native enzyme 2.1 a resolution, heavy atom derivatives diffract to 3.0 A resolution
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ARO9 by hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.6 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
-
no loss of activity after 24 h at 25C
636674
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life: 28 h
70
-
half-life: 4.2 h
110
-
half-life at pH 6.5: 30 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% glycerol and 0.0001 mM pyridoxal 5'-phosphate stabilize
-
2-oxoglutarate or pyridoxal 5'-phosphate stabilizes against heat inactivation
aromatic aminotransferase AT-1 is unstable to freeze-thaw treatment. With a single freeze-thaw cycle the enzyme loses about 50% of its original activity. Additional freeze-thaw treatments completely inactivate AT-1
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aromatic aminotransferase AT-2 is stable to repeated freeze-thaw treatments
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inactivated by freezing
-
stable to freezing and thawing
-
stable to freezing and thawing in phosphate buffers supplemented with pyridoxal phosphate, 2-oxoglutarate, dithiothreitol and EDTA
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure to 02 does not affect enzyme activity
-
721696
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM potassium phosphate buffer, pH 7.5, 10% glycerol, 10 mM DTT, 0.1 mM pyridoxal phosphate, at least 3 months, no loss of activity
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-20C, at least 3 weeks, no loss of activity
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-25C, protein concentration: 0.03-0.2 mg/ml, potassium phosphate pH 7.0, 1 mM EDTA, 1 mM dithiothreitol, 2 mM 2-oxoglutarate and 0.2 mM pyridoxal 5'-phosphate, several months, no loss of activity
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0-4C, 2 weeks, little loss of activity
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0C, 1 month, 15% loss of activity
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4C, 100 mM potassium phosphate buffer, pH 7.5, 0.002% NaN3, at least 6 months, no loss of activity
-
4C, glycerol, 10% stabilizes during storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
55C, ammonium sulfate, DE52, phenylalanine-Sepharose, Sephadex G-150
-
ammonium sulfate, 55C, 5 min, calcium phosphate gel, DEAE-cellulose, isoelectric focusing
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ammonium sulfate, DEAE-Sephacel, hydroxylapatite, Sephadex G-100, phenyl-Sepharose
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ammonium sulfate, gel filtration, anion exchange chromatography, Mono Q, phenyl-Superose
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ammonium sulfate, phenyl-Toyopearl, hydroxyapatite, Sephacryl S-200, recombinant enzyme
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ammonium sulfate, SAH-Sepharose, hydroxyapatite, pyridoxamine 5'-phosphate-Sepharose
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DEAE-cellulose, isolation of isoenzymes AAT I, AAT II and AAT III
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gramicidin S-producing strain, ammonium sulfate, heat treatment, DEAE-Sephadex, hydroxylapatite, pyridoxamine 5'-phosphate-Sepharose, Ultrogel Aca-34
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isoenzymes A and B2
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isoenzymes ArAT-I and ArAT-II, Q-Sepharose, DEAE-Sepharose, phenyl-Sepharose, Superdex-200, Mono Q
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isoenzymes AT-I and AT-II
partial; partial purification of enzyme forms ArAT-I and ArAT-II
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protamine, ammonium sulfate, DEAE-Sephadex, ultrogel AcA44, hydroxylapatite, isoelectric focusing
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Q-Sepharose, ammonium sulfate, phenyl-Sepharose, S-Sepharose
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recombinant enzyme, 80C, HiTrap Q, HiLoad superdex 200
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strain CB 60, ammonium sulfate, DEAE-cellulose, Ultrogel AcA 34, strain CB 6, DEAE-cellulose, Ultrogel AcA 34
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Streptomycin sulfate and ammonium sulfate, DEAE-Trisacryl, HA-ultrogel, Sephacryl S-200, partial purification
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vitamin B6-deficient strain, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephacryl s-200, hydroxylapatite
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of AroAT II in Escherichia coli
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overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of a fusion protein with beta-glucuronidase is upregulated in both logarithmic and stationary phases by several compounds, including indole-3-acetic acid, tryptophan, tyrosine, and phenyl acetic acid. The enzyme is expressed in bacteria associated with wheat roots. Root exudates of wheat and maize are able to stimulate expression
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y66A
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 43.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 51.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
Y66F
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.5fold lower than wild-type value
Y66L
-
mutant enzyme is able to synthesize L-diphenylalanine with 23% conversion yield for 10 h, whereas the wild-type AroATEs is inactive for the transamination between diphenylpyruvate and L-phenylalanine. kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.65fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.9fold lower than wild-type value
Y66V
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 26.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 23.1fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
Y66A
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 43.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 51.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
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Y66F
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.5fold lower than wild-type value
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Y66L
-
mutant enzyme is able to synthesize L-diphenylalanine with 23% conversion yield for 10 h, whereas the wild-type AroATEs is inactive for the transamination between diphenylpyruvate and L-phenylalanine. kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.65fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.9fold lower than wild-type value
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Y66V
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 26.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 23.1fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
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K258A
-
pKa of the Schiff base formed between the coenzyme pyridoxal 5'-phosphate and Lys258 increases by 3.6 units
R292K
-
very low activity with aspartate, 10-100fold increase in Km for aromatic amino acids
R386L
-
pKa of the Schiff base formed between the coenzyme pyridoxal 5'-phosphate and Lys258 increases by 0.7 units
nutrition
-
enzyme and branched chain amino acid transaminase are essential for conversion of aromatic and branched-chain amino acids to aroma compounds in the cheese model and also play a major role in the formation of volatile sulfur compounds from methionine
additional information
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deletion of enzyme plus branched chain amino acid transaminase, strong reduction of growth of organism in milk. Strong reduction in degradation of L-isoleucine, L-valine, L-leucine, L-methionine, L-phenylalanine, L-tryptophan
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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