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Information on EC 2.6.1.57 - aromatic-amino-acid transaminase and Organism(s) Pseudomonas aeruginosa

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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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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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, hisc1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminotransferase, aromatic amino acid
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-
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arom. amino acid transferase
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-
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arom.-amino-acid transaminase
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-
-
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aromatic amino acid aminotransferase
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aromatic amino acid transaminase
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aromatic aminotransferase
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aromatic aminotransferase AT-1
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aromatic aminotransferase AT-2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-Phe
L-Glu + phenylpyruvate
show the reaction diagram
2-oxoglutarate + Tyr
L-glutamate + 4-hydroxyphenylpyruvate
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 + Phe
tyr + phenylpyruvate
show the reaction diagram
4-hydroxyphenylpyruvate + Tyr
Tyr + 4-hydroxyphenylpyruvate
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
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 + Phe
arogenate + phenylpyruvate
show the reaction diagram
prephenate + Tyr
arogenate + 4-hydroxyphenylpyruvate
show the reaction diagram
additional information
?
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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
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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L-glutamate, aromatic aminotransferase AT-1
7
-
L-Phe, L-Tyr, L-Asp or L-Glu as substrate, aromatic aminotransferase AT-2
7.6
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L-Asp, aromatic aminotransferase AT-1
8.4
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L-Phe or L-Tyr, aromatic aminotransferase AT-1
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?
A0A485IPX3_PSEAI
59
0
6277
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
inactivated at, aromatic aminotransferase AT-1 loses activity much more precipitously than does aromatic aminotransferase AT-2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whitaker, R.J.; Gaines, C.G.; Jensen, R.A.
A multispecific quintet of aromatic aminotransferases that overlap different biochemical pathways in Pseudomonas aeruginosa
J. Biol. Chem.
257
13550-13556
1982
Pseudomonas aeruginosa
Manually annotated by BRENDA team