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)
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279
3.40.640.10 : Aspartate Aminotransferase; domain 2 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
P04693 TYRB_ECOLI An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. Homodimer. Cytoplasm. Pyridoxal phosphate.
P95468 TYRB_PARDE 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
30915
16015
PubChem 1051
51
33032
44272391
88747398
1ay4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay6B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay7A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay7B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ay9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tatF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ay4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1ay4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1ay5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Analogue:MAE
1ay5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Analogue:MAE
1ay8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1ay8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:HCI Unbound Unbound Unbound
2ay1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:AHC Unbound Unbound Unbound
2ay2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:CXP Unbound Unbound Unbound
2ay3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:MPP Unbound Unbound Unbound
2ay3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:MPP Unbound Unbound Unbound
2ay4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:PPT Unbound Unbound Unbound
2ay5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:IOP Unbound Unbound Unbound
2ay6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay6B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:3IB Unbound Unbound Unbound
2ay7A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
2ay7B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:CLT Unbound Unbound Unbound
2ay8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:4TB Unbound Unbound Unbound
2ay8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:4TB Unbound Unbound Unbound
2ay9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:5PV Unbound Unbound Unbound
2ay9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:5PV Unbound Unbound Unbound
3tatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
3tatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
3tatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
3tatD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
3tatE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
3tatF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay6B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay7A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay7B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ay9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tatF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ay4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ay4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ay5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ay5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ay8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ay8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay6B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay7A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay7B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2ay9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3tatF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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). Although the catalytic mechanism of this enzyme has not been elucidated, it must be similar to that of Aspartate aminotransferase (AAT) (D00101 in EzCatDB), as the catalytic site of this enzyme is completely the same as that.
This enzyme catalyzes transamination, which is composed of the following reactions:
(A) Formation of external aldimine (with amine group of aromatic amino acid),
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, aromatic oxo acid, and PMP.
(D) Schiff-base forming by hydration of PMP with carbonyl group of the second substrate, 2-oxoglutarate, forming a ketimine intermediate again.
(E) Isomerization (change in the position of double-bond).
(F) Formation of internal aldimine, leading to the elimination of the product,L-Glu, from PLP.

Created Updated
2004-03-25 2009-02-26