KEGG   ENZYME: 2.6.1.5Help
Entry
EC 2.6.1.5                  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
Class Transferases;
Transferring nitrogenous groups;
Transaminases
BRITE hierarchy
Sysname L-tyrosine:2-oxoglutarate aminotransferase
Reaction(IUBMB) L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
[RN:R00734]
Reaction(KEGG) R00734;
(other) R00694 R07396
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Substrate L-tyrosine [CPD:C00082];
2-oxoglutarate [CPD:C00026]
Product 4-hydroxyphenylpyruvate [CPD:C01179];
L-glutamate [CPD:C00025]
Cofactor Pyridoxal phosphate [CPD:C00018]
Comment A pyridoxal-phosphate protein. L-Phenylalanine can act instead of
L-tyrosine. The mitochondrial enzyme may be identical with EC
2.6.1.1 (aspartate transaminase). The three isoenzymic forms are
interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33
(fruit bromelain). The enzyme can also catalyse the final step in
the methionine-salvage pathway of Klebsiella pneumoniae [8].
Pathway PATH: ec00130  Ubiquinone and other terpenoid-quinone biosynthesis
PATH: ec00270  Cysteine and methionine metabolism
PATH: ec00350  Tyrosine metabolism
PATH: ec00360  Phenylalanine metabolism
PATH: ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
PATH: ec00401  Novobiocin biosynthesis
PATH: ec00950  Isoquinoline alkaloid biosynthesis
PATH: ec01061  Biosynthesis of phenylpropanoids
PATH: ec01063  Biosynthesis of alkaloids derived from shikimate
               pathway
PATH: ec01064  Biosynthesis of alkaloids derived from ornithine,
               lysine and nicotinic acid
PATH: ec01100  Metabolic pathways
Orthology KO: K00815  tyrosine aminotransferase
Genes HSA: 6898(TAT)
PTR: 454227(TAT)
MCC: 708005(TAT)
MMU: 234724(Tat)
RNO: 24813(Tat)
CFA: 479665(TAT)
BTA: 533481(TAT)
ECB: 100068116
MDO: 100020832
OAA: 100077699
GGA: 415884(TAT)
TGU: 100230394
XTR: 448486(tat)
DRE: 561410(tat)
BFO: BRAFLDRAFT_275580
CIN: 100183684
SPU: 592114
DME: Dmel_CG1461
DPO: Dpse_GA13109
DAN: Dana_GF22556
DER: Dere_GG17840
DPE: Dper_GL14927
DSE: Dsec_GM17670
DSI: Dsim_GD17166
DYA: Dyak_GE17134
DGR: Dgri_GH12929
DMO: Dmoj_GI15439
AGA: AgaP_AGAP000327
AAG: AaeL_AAEL008963
CQU: CpipJ_CPIJ003774
AME: 725204
NVI: 100119866
TCA: 659321
ISC: IscW_ISCW014463
CEL: F42D1.2
CBR: CBG07591
BMY: Bm1_31005
NVE: NEMVE_v1g207788
HMG: 100204677
TAD: TRIADDRAFT_35383
ATH: AT5G36160 AT5G53970
POP: POPTR_568851(AMT7) POPTR_594645(AMT6)
RCU: RCOM_0651460 RCOM_1173140
VVI: 100241782(GSVIVT00027735001) 100242005(GSVIVT00018628001)
     100253895(GSVIVT00018632001)
OSA: 4329098(Os02g0302400) 4329101(Os02g0302700)
SBI: SORBI_03g026220(SORBIDRAFT_03g026220)
     SORBI_05g021610(SORBIDRAFT_05g021610)
     SORBI_08g000600(SORBIDRAFT_08g000600)
ZMA: 100193424 100279205
PPP: PHYPADRAFT_215944
OLU: OSTLU_3820
CME: CMT533C
DDI: DDB_0230996(tat)
TET: TTHERM_00046180 TTHERM_00554320 TTHERM_00683360
PTM: GSPATT00003669001
TCR: 508535.50 510187.20 510187.30 510187.40 510187.50 510187.70
     510795.10 511461.20
LMA: LmjF36.2360
LIF: LinJ36.4910
LBZ: LbrM35_V2.2580
PTI: PHATR_51609
TPS: THAPSDRAFT_268594
Taxonomy
Structures PDB: 1BW0  3DYD  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:13366978]
CANELLAKIS ZN, COHEN PP.
Purification studies of tyrosine-alpha-ketoglutaric acid
transaminase.
J. Biol. Chem. 222 (1956) 53-62.
Canis familiaris [GN:cfa]
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:13366979]
CANELLAKIS ZN, COHEN PP.
Kinetic and substrate specificity study of
tyrosine-alpha-ketoglutaric acid transaminase.
J. Biol. Chem. 222 (1956) 63-71.
Canis familiaris [GN:cfa]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:14171223]
JACOBY GA, LADU BN.
STUDIES ON THE SPECIFICITY OF TYROSINE-ALPHA-KETOGLUTARATE
TRANSAMINASE.
J. Biol. Chem. 239 (1964) 419-24.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:14408534]
KENNEY FT.
Properties of partially purified tyrosine-alpha-ketoglutarate
transaminase from rat liver.
J. Biol. Chem. 234 (1959) 2707-12.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
5  [PMID:4396841]
Miller JE, Litwack G.
Purification, properties, and identity of liver mitochondrial
tyrosine aminotransferase.
J. Biol. Chem. 246 (1971) 3234-40.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
6  [PMID:13363833]
ROWSELL EV.
Transaminations with L-glutamate and alpha-oxoglutarate in fresh
extracts of animal tissues.
Biochem. J. 64 (1956) 235-45.
Sus scofa [GN:ssc]
Reference
  Authors
  Title

  Journal
  Organism
7  [PMID:13750129]
SENTHESHANMUGANATHAN S.
The purification and properties of the tyrosine-2-oxoglutarate
transaminase of Saccharomyces cerevisiae.
Biochem. J. 77 (1960) 619-25.
Canis familiaris [GN:cfa], Saccharomyces cerevisiae [GN:sce]
Reference
  Authors
  Title

  Journal
  Organism
8  [PMID:10074065]
Heilbronn J, Wilson J, Berger BJ.
Tyrosine aminotransferase catalyzes the final step of methionine
recycling in Klebsiella pneumoniae.
J. Bacteriol. 181 (1999) 1739-47.
Klebsiella pneumoniae [GN:kpn]
Other DBs ExplorEnz - The Enzyme Database: 2.6.1.5
IUBMB Enzyme Nomenclature: 2.6.1.5
ExPASy - ENZYME nomenclature database: 2.6.1.5
UM-BBD (Biocatalysis/Biodegradation Database): 2.6.1.5
BRENDA, the Enzyme Database: 2.6.1.5
CAS: 9014-55-5

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