EzCatDB: D00102
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DB codeD00102
RLCP classification6.30.97700.5320 : 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 domainDomain 13.90.1150.10 : Aspartate Aminotransferase, domain 1
Domain 23.40.640.10 : Aspartate Aminotransferase; domain 2Catalytic domain
E.C.2.6.1.5

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

Enzyme Name
UniProtKBKEGG

P33447
Protein nameTyrosine aminotransferasetyrosine 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
SynonymsTAT
EC 2.6.1.5
L-tyrosine:2-oxoglutarate aminotransferase
PfamPF00155 (Aminotran_1_2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00271Methionine metabolism
MAP00350Tyrosine metabolism
MAP00360Phenylalanine metabolism
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis
MAP00401Novobiocin biosynthesis
MAP00950Alkaloid biosynthesis I

UniProtKB:Accession NumberP33447
Entry nameATTY_TRYCR
ActivityL-tyrosine + 2-oxoglutarate = 4- hydroxyphenylpyruvate + L-glutamate.
SubunitHomodimer.
Subcellular locationCytoplasm. Mitochondrion. Note=Mainly cytoplasmic. Present to a small extent in the mitochondrial fraction.
CofactorPyridoxal phosphate.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00018C00082C00026C01179C00025I00025I00035I00026
C00647I00006I00033I00007
CompoundPyridoxal phosphateL-Tyrosine2-Oxoglutarate4-HydroxyphenylpyruvateL-GlutamateExternal 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)
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,aromatic ring (only carbon atom)carbohydrate,carboxyl grouparomatic ring (only carbon atom),carbohydrate,carboxyl groupamino acids,carboxyl group







ChEBI18405
17895
58315
30915
15999
16015








PubChem1051
6942100
6057
51
979
88747398
44272391
33032








                     
1bw0A01UnboundUnboundUnboundUnboundUnbound        
1bw0B01UnboundUnboundUnboundUnboundUnbound        
1bw0A02Bound:LLPUnboundUnboundUnboundUnbound        
1bw0B02Bound:LLPUnboundUnboundUnboundUnbound        

Active-site residues
pdbCatalytic residuesModified residuescomment
           
1bw0A01 
 
 
1bw0B01 
 
 
1bw0A02TYR 71;ASP 216;TYR 219
LLP 253
modified PLP binding Lys 253
1bw0B02TYR 71;ASP 216;TYR 219
LLP 253
modified PLP binding Lys 253

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[11]Fig.4, p.2408-2410

references
[1]
PubMed ID4384332
JournalBiochim Biophys Acta
Year1968
Volume151
Pages88-98
AuthorsIgo RP, Mahoney CP, Limbeck GA
TitleStudies on tyrosine-alpha-ketoglutarate transaminase from bovine thyroid and liver tissue.
[2]
PubMed ID4146264
JournalJ Biol Chem
Year1973
Volume248
Pages4528-31
AuthorsJohnson RW, Kenney FT
TitleRegulation of tyrosine aminotransferase in rat liver. XI. Studies on the relationship of enzyme stability to enzyme turnover in cultured hepatoma cells.
[3]
PubMed ID237848
JournalInt Rev Neurobiol
Year1975
Volume17
Pages85-129
AuthorsBenuck M, Lajtha A
TitleAminotransferase activity in brain.
[4]
PubMed ID469
JournalJ Neurochem
Year1975
Volume25
Pages579-82
AuthorsNoguchi T, Nakatani M, Minatogawa Y, Okuno E, Kido R
TitleCerebral aromatic aminotransferase.
[5]
PubMed ID1682148
JournalEur J Biochem
Year1991
Volume201
Pages399-407
AuthorsDietrich JB, Lorber B, Kern D
TitleExpression of mammalian tyrosine aminotransferase in Saccharomyces cerevisiae and Escherichia coli. Purification to homogeneity and characterization of the enzyme overproduced in the bacteria.
[6]
PubMed ID1353027
JournalFEBS Lett
Year1992
Volume306
Pages234-8
AuthorsJager J, Solmajer T, Jansonius JN
TitleComputational approach towards the three-dimensional structure of E. coli tyrosine aminotransferase.
[7]
PubMed ID7703851
JournalProtein Sci
Year1994
Volume3
Pages2055-63
AuthorsMatsuo Y, Nishikawa K
TitleProtein structural similarities predicted by a sequence-structure compatibility method.
[8]
PubMed ID7664122
JournalNat Struct Biol
Year1995
Volume2
Pages548-53
AuthorsMalashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN
TitleAlternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
[9]
PubMed ID9761826
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages105-7
AuthorsNowicki C, Montemartini M, Hunter GR, Blankenfeldt W, Kalisz HM, Hecht HJ
TitleCrystallization and preliminary X-ray analysis of tyrosine aminotransferase from Trypanosoma cruzi epimastigotes.
[10]
PubMed ID10417420
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages1474-7
AuthorsKo TP, Wu SP, Yang WZ, Tsai H, Yuan HS
TitleCrystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID20060992
PubMed ID10595543
JournalProtein Sci
Year1999
Volume8
Pages2406-17
AuthorsBlankenfeldt W, Nowicki C, Montemartini-Kalisz M, Kalisz HM, Hecht HJ
TitleCrystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode.
Related PDB1bw0
Related UniProtKBP33447

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.

createdupdated
2004-03-172009-02-26


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