DB code: D00102

RLCP classification 6.40.521000.5530 : Double-bonded atom exchange
8.211.591510.5527 : Isomerization
6.10.82600.5900 : Double-bonded atom exchange
6.20.85200.5520 : Double-bonded atom exchange
8.211.591510.5526 : Isomerization
6.30.97700.5320 : 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. 2.6.1.5
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P33447 Tyrosine aminotransferase
TAT
EC 2.6.1.5
L-tyrosine:2-oxoglutarate aminotransferase
PF00155 (Aminotran_1_2)
[Graphical View]

KEGG enzyme name
tyrosine transaminase
tyrosine aminotransferase
glutamic-hydroxyphenylpyruvic transaminase
glutamic phenylpyruvic aminotransferase
L-phenylalanine 2-oxoglutarate aminotransferase
L-tyrosine aminotransferase
phenylalanine aminotransferase
phenylalanine transaminase
phenylalanine-alpha-ketoglutarate transaminase
phenylpyruvate transaminase
phenylpyruvic acid transaminase
tyrosine-alpha-ketoglutarate aminotransferase
tyrosine-alpha-ketoglutarate transaminase
tyrosine-2-ketoglutarate aminotransferase
TyrAT

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P33447 ATTY_TRYCR L-tyrosine + 2-oxoglutarate = 4- hydroxyphenylpyruvate + L-glutamate. Homodimer. Cytoplasm. Mitochondrion. Note=Mainly cytoplasmic. Present to a small extent in the mitochondrial fraction. 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 C00082 C00026 C01179 C00025 I00025 I00035 I00026 C00647 I00006 I00033 I00007
E.C. (carbinolabine)
Compound Pyridoxal phosphate L-Tyrosine 2-Oxoglutarate 4-Hydroxyphenylpyruvate L-Glutamate External aldimine intermediate (initial stage:PLP-Tyr) Quinonoid intermediate-1 (PLP-Tyr) Ketimine intermediate-1 (PLP-Tyr) 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
58315
17895
30915
15999
16015
PubChem 1051
6942100
6057
51
979
88747398
44272391
33032
1bw0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bw0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bw0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:LLP Unbound Unbound Unbound Unbound
1bw0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:LLP Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bw0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bw0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bw0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 71;ASP 216;TYR 219 LLP 253 modified PLP binding Lys 253
1bw0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 71;ASP 216;TYR 219 LLP 253 modified PLP binding Lys 253

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[11]
Fig.4, p.2408-2410

References
[1]
Resource
Comments
Medline ID
PubMed ID 4384332
Journal Biochim Biophys Acta
Year 1968
Volume 151
Pages 88-98
Authors Igo RP, Mahoney CP, Limbeck GA
Title Studies on tyrosine-alpha-ketoglutarate transaminase from bovine thyroid and liver tissue.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 4146264
Journal J Biol Chem
Year 1973
Volume 248
Pages 4528-31
Authors Johnson RW, Kenney FT
Title Regulation of tyrosine aminotransferase in rat liver. XI. Studies on the relationship of enzyme stability to enzyme turnover in cultured hepatoma cells.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 237848
Journal Int Rev Neurobiol
Year 1975
Volume 17
Pages 85-129
Authors Benuck M, Lajtha A
Title Aminotransferase activity in brain.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 469
Journal J Neurochem
Year 1975
Volume 25
Pages 579-82
Authors Noguchi T, Nakatani M, Minatogawa Y, Okuno E, Kido R
Title Cerebral aromatic aminotransferase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1682148
Journal Eur J Biochem
Year 1991
Volume 201
Pages 399-407
Authors Dietrich JB, Lorber B, Kern D
Title Expression of mammalian tyrosine aminotransferase in Saccharomyces cerevisiae and Escherichia coli. Purification to homogeneity and characterization of the enzyme overproduced in the bacteria.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1353027
Journal FEBS Lett
Year 1992
Volume 306
Pages 234-8
Authors Jager J, Solmajer T, Jansonius JN
Title Computational approach towards the three-dimensional structure of E. coli tyrosine aminotransferase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7703851
Journal Protein Sci
Year 1994
Volume 3
Pages 2055-63
Authors Matsuo Y, Nishikawa K
Title Protein structural similarities predicted by a sequence-structure compatibility method.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7664122
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 548-53
Authors Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN
Title Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9761826
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 105-7
Authors Nowicki C, Montemartini M, Hunter GR, Blankenfeldt W, Kalisz HM, Hecht HJ
Title Crystallization and preliminary X-ray analysis of tyrosine aminotransferase from Trypanosoma cruzi epimastigotes.
Related PDB
Related UniProtKB
[10]
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
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 20060992
PubMed ID 10595543
Journal Protein Sci
Year 1999
Volume 8
Pages 2406-17
Authors Blankenfeldt W, Nowicki C, Montemartini-Kalisz M, Kalisz HM, Hecht HJ
Title Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode.
Related PDB 1bw0
Related UniProtKB P33447

Comments
This enzyme belongs to the Aspartate aminotransferase (AAT) subclass of type-I PLP-dependent enzyme superfamily (Aspartate aminotransferase superfamily; AAT subclass I). Since this enzyme is homologous to aspartate aminotransferase (D00101 in EzCatDB), with conserved catalytic residues, this enzyme must have the same catalytic reaction mechanism to that of the homologue.
This enzyme catalyzes transamination, which is composed of the following reactions:
(A) Formation of external aldimine (with amine group of L-Tyrosine),
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, hydroxyphenylpyruvate, 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 from PLP.

Created Updated
2004-03-17 2009-02-26