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Information on EC 2.6.1.57 - aromatic-amino-acid transaminase and Organism(s) Paracoccus denitrificans and UniProt Accession P95468

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.57 aromatic-amino-acid transaminase
IUBMB Comments
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.
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Paracoccus denitrificans
UNIPROT: P95468
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The taxonomic range for the selected organisms is: Paracoccus denitrificans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aromatic aminotransferase, aromatic amino acid aminotransferase, aroat, pdaroat, aromatic-amino-acid aminotransferase, yer152c, pdarat, aromatic aminotransferase ii, aromatic amino acid transaminase, aratph, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aromatic amino acid aminotransferase
-
aminotransferase, aromatic amino acid
-
-
-
-
arom. amino acid transferase
-
-
-
-
arom.-amino-acid transaminase
-
-
-
-
aromatic amino acid aminotransferase
-
-
-
-
aromatic amino acid transaminase
-
-
-
-
aromatic aminotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aspartate + 3-phenylpyruvate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
L-aspartate + 3-(4-hydroxyphenyl)pyruvate
L-tyrosine + oxaloacetate
show the reaction diagram
-
-
r
L-cysteine + 2-oxoglutarate
3-mercaptopyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
enzyme also reacts with 2-aminooctanoate and 2-aminoheptanoate
-
r
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
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-phenylbutyric acid
-
5-phenylvaleric acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 0.59
2-oxoglutarate
0.059
3-(4-hydroxyphenyl)pyruvate
pH 8.0, 25°C, cosubstrate aspartate
0.079 - 1.8
L-aspartate
12.22
L-cysteine
at pH 7.4 and 30°C
1.4
L-tryptophan
pH 8.0, 25°C, cosubstrate 2-oxoglutarate
0.083
phenylpyruvate
pH 8.0, 25°C, cosubstrate aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.9
L-aspartate
at pH 7.4 and 30°C
16.89
L-cysteine
at pH 7.4 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
214
L-aspartate
at pH 7.4 and 30°C
1.4
L-cysteine
at pH 7.4 and 30°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYRB_PARDE
394
0
42732
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42653
2 * 42653, mass spectrometry
42731
2 * 42731, deduced from nucleotide sequence
83000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, phenyl-Toyopearl, hydroxyapatite, Sephacryl S-200, recombinant enzyme
His SpinTrap column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oue, S.; Okamoto, A.; Nakai, Y.; Nakahira, M.; Shibatani, T.; Hayashi, H.; Kagamiyama, H.
Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism
J. Biochem.
121
161-171
1997
Paracoccus denitrificans (P95468), Paracoccus denitrificans
Manually annotated by BRENDA team
Okamoto, A.; Nakai, Y.; Hayashi, H.; Hirotsu, K.; Kagamiyama, H.
Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network
J. Mol. Biol.
280
443-461
1998
Paracoccus denitrificans (P95468), Paracoccus denitrificans
Manually annotated by BRENDA team
Okamoto, A.; Ishii, S.; Hirotsu, K.; Kagamiyama, H.
The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity
Biochemistry
38
1176-1184
1999
Paracoccus denitrificans (P95468), Paracoccus denitrificans
Manually annotated by BRENDA team
Andreessen, C.; Gerlt, V.; Steinbuechel, A.
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Enzyme Microb. Technol.
99
38-48
2017
Cupriavidus necator, Escherichia coli (P04693), Escherichia coli MG1655 (P04693), Paracoccus denitrificans (P95468), Paracoccus denitrificans Pd1222 (P95468), Shimwellia blattae, Shimwellia blattae ATCC 33430
Manually annotated by BRENDA team