DB code: D00108
| RLCP classification | 6.30.97700.5320 : Double-bonded atom exchange | |
|---|---|---|
| 8.211.591510.5526 : Isomerization | ||
| 6.20.85200.5520 : Double-bonded atom exchange | ||
| 6.10.82600.5900 : Double-bonded atom exchange | ||
| 8.211.591510.5527 : Isomerization | ||
| 6.40.521000.5530 : Double-bonded atom exchange | ||
| CATH domain | 3.90.1150.10 : Aspartate Aminotransferase, domain 1 | |
| 3.40.640.10 : Aspartate Aminotransferase; domain 2 | Catalytic domain | |
| E.C. | 2.6.1.57 | |
| CSA | 1ay4 | |
| M-CSA | 1ay4 | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.640.10 : Aspartate Aminotransferase; domain 2 | D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279 |
| 3.90.1150.10 : Aspartate Aminotransferase, domain 1 | D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam | RefSeq |
|---|---|---|---|---|
| P95468 |
Aromatic-amino-acid aminotransferase
|
ARAT
AROAT EC 2.6.1.57 |
PF00155
(Aminotran_1_2)
[Graphical View] |
|
| P04693 |
Aromatic-amino-acid aminotransferase
|
ARAT
AROAT EC 2.6.1.57 |
PF00155
(Aminotran_1_2)
[Graphical View] |
NP_418478.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_492197.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
| KEGG enzyme name |
|---|
|
aromatic-amino-acid transaminase
aromatic amino acid aminotransferase aromatic aminotransferase ArAT |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P95468 | TYRB_PARDE | An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. | Homodimer. | Cytoplasm. | Pyridoxal phosphate. |
| P04693 | TYRB_ECOLI | An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. | Homodimer. | Cytoplasm. | Pyridoxal phosphate. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00271 | Methionine metabolism | |
| MAP00350 | Tyrosine metabolism | |
| MAP00360 | Phenylalanine metabolism | |
| MAP00400 | Phenylalanine, tyrosine and tryptophan biosynthesis | |
| MAP00401 | Novobiocin biosynthesis | |
| MAP00950 | Alkaloid biosynthesis I |
| Compound table | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||||||
| KEGG-id | C00018 | C01021 | C00026 | C00972 | C00025 | I00027 | I00036 | I00028 | C00647 | I00006 | I00033 | I00007 | ||||||
| E.C. |
(carbinolabine)
|
|||||||||||||||||
| Compound | Pyridoxal phosphate | Aromatic amino acid | 2-Oxoglutarate | Aromatic oxo acid | L-Glutamate | External aldimine intermediate (initial stage:PLP-aromatic amino acid) | Quinonoid intermediate-1 (PLP-aromatic amino acid) | Ketimine intermediate-1 (PLP-aromatic amino acid) | Tetrahedral intermediate from ketimine to PMP | Pyridoxamine phosphate (PMP) | Ketimine intermediate-2 (PLP-Glu) | Quinonoid intermediate-2 (PLP-Glu) | External aldimine intermediate (final stage:PLP-Glu) | |||||
| Type | aromatic ring (with nitrogen atoms),phosphate group/phosphate ion | amino acids,aromatic ring (only carbon atom) | carbohydrate,carboxyl group | aromatic ring (only carbon atom),carbohydrate,carboxyl group | amino acids,carboxyl group | |||||||||||||
| ChEBI |
18405 18405 |
30915 30915 |
16015 16015 |
|||||||||||||||
| PubChem |
1051 1051 |
51 51 |
33032 44272391 88747398 33032 44272391 88747398 |
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| 1ay4A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay4B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay5A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay5B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay8A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay8B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay1A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay1B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay2A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay2B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay3A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay3B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay4A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay4B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay5A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay5B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay6A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay6B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay7A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay7B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay8A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay8B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay9A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay9B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatE01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatF01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay4A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay4B02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay5A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Analogue:MAE | ||||||||
| 1ay5B02 |
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Bound:PLP | Unbound | Unbound | Unbound | Analogue:MAE | ||||||||
| 1ay8A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 1ay8B02 |
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Bound:PLP | Analogue:HCI | Unbound | Unbound | Unbound | ||||||||
| 2ay1A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay1B02 |
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Bound:PLP | Analogue:AHC | Unbound | Unbound | Unbound | ||||||||
| 2ay2A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay2B02 |
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Bound:PLP | Analogue:CXP | Unbound | Unbound | Unbound | ||||||||
| 2ay3A02 |
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Bound:PLP | Analogue:MPP | Unbound | Unbound | Unbound | ||||||||
| 2ay3B02 |
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Bound:PLP | Analogue:MPP | Unbound | Unbound | Unbound | ||||||||
| 2ay4A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay4B02 |
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Bound:PLP | Analogue:PPT | Unbound | Unbound | Unbound | ||||||||
| 2ay5A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay5B02 |
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Bound:PLP | Analogue:IOP | Unbound | Unbound | Unbound | ||||||||
| 2ay6A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay6B02 |
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Bound:PLP | Analogue:3IB | Unbound | Unbound | Unbound | ||||||||
| 2ay7A02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 2ay7B02 |
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Bound:PLP | Analogue:CLT | Unbound | Unbound | Unbound | ||||||||
| 2ay8A02 |
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Bound:PLP | Analogue:4TB | Unbound | Unbound | Unbound | ||||||||
| 2ay8B02 |
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Bound:PLP | Analogue:4TB | Unbound | Unbound | Unbound | ||||||||
| 2ay9A02 |
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Bound:PLP | Analogue:5PV | Unbound | Unbound | Unbound | ||||||||
| 2ay9B02 |
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Bound:PLP | Analogue:5PV | Unbound | Unbound | Unbound | ||||||||
| 3tatA02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatB02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatC02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatD02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatE02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| 3tatF02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | ||||||||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| PDB;1ay4 and literature [2], [5] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1ay4A01 |
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| 1ay4B01 |
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| 1ay5A01 |
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| 1ay5B01 |
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| 1ay8A01 |
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| 1ay8B01 |
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| 2ay1A01 |
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| 2ay1B01 |
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| 2ay2A01 |
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| 2ay2B01 |
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| 2ay3A01 |
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| 2ay3B01 |
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| 2ay4A01 |
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| 2ay4B01 |
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| 2ay5A01 |
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| 2ay5B01 |
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| 2ay6A01 |
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| 2ay6B01 |
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| 2ay7A01 |
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| 2ay7B01 |
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| 2ay8A01 |
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| 2ay8B01 |
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| 2ay9A01 |
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| 2ay9B01 |
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| 3tatA01 |
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| 3tatB01 |
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| 3tatC01 |
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| 3tatD01 |
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| 3tatE01 |
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| 3tatF01 |
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| 1ay4A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 1ay4B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 1ay5A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 1ay5B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 1ay8A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 1ay8B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay1A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay1B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay2A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay2B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay3A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay3B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay4A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay4B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay5A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay5B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay6A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay6B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay7A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay7B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay8A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay8B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay9A02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 2ay9B02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatA02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatB02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatC02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatD02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatE02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| 3tatF02 |
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TYR 70;ASP 222;TYR 225;LYS 258 | LYS 258(PLP binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[10]
|
Scheme 1 | |
|
[12]
|
Fig. 1, p.376 | |
|
[12]
|
Fig. 2, p.377 | |
|
[12]
|
Fig. 3, p.378 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8218300 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 12229-39 |
| Authors | Hayashi H, Inoue K, Nagata T, Kuramitsu S, Kagamiyama H |
| Title | Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8188625 |
| Journal | J Biochem (Tokyo) |
| Year | 1994 |
| Volume | 115 |
| Pages | 156-61 |
| Authors | Iwasaki M, Hayashi H, Kagamiyama H |
| Title | Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8639626 |
| Journal | Biochemistry |
| Year | 1996 |
| Volume | 35 |
| Pages | 6754-61 |
| Authors | Hayashi H, Inoue K, Mizuguchi H, Kagamiyama H |
| Title | Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9058208 |
| Journal | J Biochem (Tokyo) |
| Year | 1997 |
| Volume | 121 |
| Pages | 161-71 |
| Authors | Oue S, Okamoto A, Nakai Y, Nakahira M, Shibatani T, Hayashi H, Kagamiyama H |
| Title | Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9660802 |
| Journal | J Biol Chem |
| Year | 1998 |
| Volume | 273 |
| Pages | 18353-64 |
| Authors | Kawaguchi S, Kuramitsu S |
| Title | Thermodynamics and molecular simulation analysis of hydrophobic substrate recognition by aminotransferases. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) |
| Medline ID | 98332746 |
| PubMed ID | 9665848 |
| Journal | J Mol Biol |
| Year | 1998 |
| Volume | 280 |
| Pages | 443-61 |
| Authors | Okamoto A, Nakai Y, Hayashi H, Hirotsu K, Kagamiyama H |
| Title | Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. |
| Related PDB | 1ay4 1ay5 1ay8 |
| Related UniProtKB | P95468 |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9846749 |
| Journal | Microbiology |
| Year | 1998 |
| Volume | 144 |
| Pages | 3127-34 |
| Authors | Gu W, Song J, Bonner CA, Xie G, Jensen RA |
| Title | PhhC is an essential aminotransferase for aromatic amino acid catabolism in Pseudomonas aeruginosa. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) |
| Medline ID | 99130247 |
| PubMed ID | 9930977 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 1176-84 |
| Authors | Okamoto A, Ishii S, Hirotsu K, Kagamiyama H |
| Title | The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity. |
| Related PDB | 2ay1 2ay2 2ay3 2ay4 2ay5 2ay6 2ay7 2ay8 2ay9 |
| Related UniProtKB | P95468 |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10417420 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 1999 |
| Volume | 55 |
| Pages | 1474-7 |
| Authors | Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS |
| Title | Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. |
| Related PDB | 3tat |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11112527 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 15418-28 |
| Authors | Islam MM, Hayashi H, Mizuguchi H, Kagamiyama H |
| Title | The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10671523 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 4871-9 |
| Authors | Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K |
| Title | The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11933244 |
| Journal | Chem Rec |
| Year | 2001 |
| Volume | 1 |
| Pages | 373-84 |
| Authors | Soda K, Yoshimura T, Esaki N |
| Title | Stereospecificity for the hydrogen transfer of pyridoxal enzyme reactions. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the Aspartate aminotransferase (AAT) subclass of type-I PLP-dependent enzyme superfamily (Aspartate aminotransferase superfamily; AAT). This enzyme catalyzes transamination, (A) Formation of external aldimine (with amine group of aromatic amino acid), (B) Isomerization (change in the position of double-bond), (C) Schiff-base deforming by hydration, (D) Schiff-base forming by hydration of PMP with carbonyl group of the second substrate, (E) Isomerization (change in the position of double-bond). (F) Formation of internal aldimine, |
| Created | Updated |
|---|---|
| 2004-03-25 | 2009-02-26 |