Information on EC 2.6.1.57 - aromatic-amino-acid transaminase

Word Map on EC 2.6.1.57
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, 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
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
Isoquinoline alkaloid 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)
-
-
Lysine biosynthesis
-
-
Metabolic pathways
-
-
Novobiocin biosynthesis
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
rosmarinic acid biosynthesis I
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
Tyrosine metabolism
-
-
methionine metabolism
-
-
phenylalanine metabolism
-
-
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
-
Q5ACW9, Q5ADA2
UniProt
Manually annotated by BRENDA team
-
Q5ACW9, Q5ADA2
UniProt
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
-
-
-
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 + L-phenylalanine
L-glutamate + phenylpyruvate
show the reaction diagram
2-oxoglutarate + L-tryptophan
L-glutamate + indolepyruvate
show the reaction diagram
2-oxoglutarate + Phe
L-glutamate + phenylpyruvate
show the reaction diagram
2-oxoglutarate + Trp
L-glutamate + 3-indole-2-oxopropanoate
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-glutamate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
Q5ACW9, Q5ADA2
-
-
-
?
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-oxoadipate
phenylpyruvate + L-2-aminoadipate
show the reaction diagram
Q5ACW9, Q5ADA2
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
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
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
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 + L-tryptophan
L-aspartate + indolepyruvate
show the reaction diagram
oxaloacetate + Phe
Asp + phenylpyruvate
show the reaction diagram
oxaloacetate + Tyr
Asp + 4-hydroxyphenylpyruvate
show the reaction diagram
oxaloaspartate + Ile
L-Asp + 3-methyl-2-oxo-pentanoate
show the reaction diagram
at 2.5 mM, 7.1% of the amine donor activity of Phe
-
-
?
oxoglutarate + Ile
L-Asp + 3-methyl-2-oxo-pentanoate
show the reaction diagram
Ile, at 2.5 mM, 14.9% of the amine donor activity of Phe
-
-
?
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 + L-Asp
Phe + oxaloacetate
show the reaction diagram
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
show the reaction diagram
Q5ACW9, Q5ADA2
-
-
-
?
phenylpyruvate + Phe
Phe + phenylpyruvate
show the reaction diagram
phenylpyruvate + Tyr
Phe + 3-(4-hydroxyphenyl)-2-oxopropanoic acid
show the reaction diagram
phenylpyruvate + Tyr
Phe + 4-hydroxyphenylpyruvate
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
pyruvate + L-tryptophan
L-alanine + indolepyruvate
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, 37°C
0.1
2-oxoadipate
Q5ACW9, Q5ADA2
pH 7.0, 22°C
0.14 - 38
2-oxoglutarate
0.059
3-(4-hydroxyphenyl)pyruvate
-
pH 8.0, 25°C, cosubstrate aspartate
0.03 - 0.05
4-hydroxyphenylpyruvate
0.33
alpha-ketomethiobutyrate
7.04
glyoxylate
Q5ACW9, Q5ADA2
pH 7.0, 22°C
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, 37°C, AAT I
1.8 - 8.4
L-aspartate
0.28
L-glutamate
-
pH 7.6, 37°C
7
L-glutamine
-
pH 8.6, 37°C, AAT I
0.35 - 70
L-histidine
4 - 7.1
L-leucine
1.5 - 5
L-methionine
0.05 - 16.6
L-phenylalanine
0.095 - 16.6
L-tryptophan
0.042 - 15
L-tyrosine
0.12 - 5.1
oxaloacetate
2.18
phenylalanine
0.01 - 0.083
phenylpyruvate
0.08
prephenate
-
pH 8.6, 37°C, AAT I
0.001 - 0.025
pyridoxal 5'-phosphate
3.59 - 8.8
pyruvate
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, 37°C
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 95°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 95
-
extremely thermostable aromatic aminotransferase from hyperthermophilic archaeon, very low activity at 30°C, approx. 50% of maximal activity at 65°C
30 - 105
-
virtually inactive at 30°C, approx. 50% of maximal ArAT-I activity at 70°C, approx. 50% of ArAT-II activity at 80°C, isoenzymes ArAT-I and II
37 - 80
-
37°C: about 35% of maximal activity, 50°C: about 90% of maximal activity, 80°C: 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
33000
-
2 * 33000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
42653
-
2 * 42653, mass spectrometry
42731
-
2 * 42731, deduced from nucleotide sequence
43000
-
2 * 43000, SDS-PAGE
43537
-
2 * 43537, deduced from nucleotide sequence
45000
-
2 * 45000, ArAT-II, SDS-PAGE
46300
x * 46300, calculated
47000
-
2 * 47000, ArAT-I, SDS-PAGE
52000
-
2 * 52000, SDS-PAGE
53000
-
gel filtration
55000 - 59000
-
-
55000
Q5ACW9, Q5ADA2
PAGE
56000
-
recombinant enzyme, gel filtration
63000
Q5ACW9, Q5ADA2
gel filtration
63500
-
gel filtration
68000
-
x * 46000, x * 68000, x * 86000, SDS-PAGE of 3 isoforms
69500
Q5ACW9, Q5ADA2
PAGE
71000
-
gel filtration
73500
Q5ACW9, Q5ADA2
gel filtration
84000
-
homodimeric form, gel filtration
85000
-
isoenzyme AAT-II, gel filtration
86000
-
x * 46000, x * 68000, x * 86000, SDS-PAGE of 3 isoforms
97000
Q5ACW9, Q5ADA2
PAGE
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
monomer
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
-
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 25°C
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
-
aromatic aminotransferase AT-2 is stable to repeated freeze-thaw treatments
-
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure to 02 does not affect enzyme activity
-
721696
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 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
-
-20°C, at least 3 weeks, no loss of activity
-
-25°C, 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
-
0-4°C, 2 weeks, little loss of activity
-
0°C, 1 month, 15% loss of activity
-
4°C, 100 mM potassium phosphate buffer, pH 7.5, 0.002% NaN3, at least 6 months, no loss of activity
-
4°C, glycerol, 10% stabilizes during storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
55°C, ammonium sulfate, DE52, phenylalanine-Sepharose, Sephadex G-150
-
ammonium sulfate, 55°C, 5 min, calcium phosphate gel, DEAE-cellulose, isoelectric focusing
-
ammonium sulfate, DEAE-Sephacel, hydroxylapatite, Sephadex G-100, phenyl-Sepharose
-
ammonium sulfate, gel filtration, anion exchange chromatography, Mono Q, phenyl-Superose
-
ammonium sulfate, phenyl-Toyopearl, hydroxyapatite, Sephacryl S-200, recombinant enzyme
-
ammonium sulfate, SAH-Sepharose, hydroxyapatite, pyridoxamine 5'-phosphate-Sepharose
-
DEAE-cellulose, isolation of isoenzymes AAT I, AAT II and AAT III
-
gramicidin S-producing strain, ammonium sulfate, heat treatment, DEAE-Sephadex, hydroxylapatite, pyridoxamine 5'-phosphate-Sepharose, Ultrogel Aca-34
-
isoenzymes A and B2
-
isoenzymes ArAT-I and ArAT-II, Q-Sepharose, DEAE-Sepharose, phenyl-Sepharose, Superdex-200, Mono Q
-
isoenzymes AT-I and AT-II
partial; partial purification of enzyme forms ArAT-I and ArAT-II
-
protamine, ammonium sulfate, DEAE-Sephadex, ultrogel AcA44, hydroxylapatite, isoelectric focusing
-
Q-Sepharose, ammonium sulfate, phenyl-Sepharose, S-Sepharose
-
recombinant enzyme, 80°C, HiTrap Q, HiLoad superdex 200
-
strain CB 60, ammonium sulfate, DEAE-cellulose, Ultrogel AcA 34, strain CB 6, DEAE-cellulose, Ultrogel AcA 34
-
Streptomycin sulfate and ammonium sulfate, DEAE-Trisacryl, HA-ultrogel, Sephacryl S-200, partial purification
-
vitamin B6-deficient strain, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephacryl s-200, hydroxylapatite
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
Q5ACW9, Q5ADA2
expression of AroAT II in Escherichia coli
-
overexpression in Escherichia coli
-