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
Show
Substrate
L-tyrosine [CPD:C00082];
2-oxoglutarate [CPD:C00026]
Product
4-hydroxyphenylpyruvate [CPD:C01179];
L-glutamate [CPD:C00025]
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].
History
EC 2.6.1.5 created 1961
Pathway
Ubiquinone and other terpenoid-quinone biosynthesis
Cysteine and methionine metabolism
Tyrosine metabolism
Phenylalanine metabolism
Phenylalanine, tyrosine and tryptophan biosynthesis
Novobiocin biosynthesis
Isoquinoline alkaloid biosynthesis
Tropane, piperidine and pyridine alkaloid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00815  
tyrosine aminotransferase
K00838  
aromatic amino acid aminotransferase I
Genes
HSA: 
6898(TAT)
PTR: 
454227(TAT)
PPS: 
GGO: 
PON: 
MCC: 
708005(TAT)
MCF: 
MMU: 
234724(Tat)
RNO: 
24813(Tat)
CGE: 
HGL: 
TUP: 
CFA: 
479665(TAT)
AML: 
FCA: 
PTG: 
BTA: 
533481(TAT)
BOM: 
PHD: 
CHX: 
SSC: 
CFR: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
415884(TAT)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
PSS: 
CMY: 
ACS: 
XTR: 
448486(tat)
DRE: 
561410(tat)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
725204(GB15166)
NVI: 
TCA: 
BMOR: 
PHU: 
ISC: 
CEL: 
CELE_F42D1.2(tatn-1)
CBR: 
BMY: 
LOA: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
MTR: 
CAM: 
FVE: 
CSV: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os02t0302200-01(Os02g0302200) Os02t0302700-01(Os02g0302700) Os02t0306401-00(Os02g0306401) Os06t0345200-01(Os06g0345200) Os11t0552000-01(Os11g0552000) Os11t0644800-00(Os11g0644800)
OBR: 
BDI: 
SBI: 
SORBI_02g003520(SORBIDRAFT_02g003520) SORBI_03g026220(SORBIDRAFT_03g026220) SORBI_05g021600(SORBIDRAFT_05g021600) SORBI_05g021610(SORBIDRAFT_05g021610) SORBI_08g000600(SORBIDRAFT_08g000600)
ZMA: 
SITA: 
ATR: 
s00127p00041670(AMTR_s00127p00041670)
SMO: 
PPP: 
OLU: 
OTA: 
MIS: 
MPP: 
CME: 
GSL: 
CCP: 
SCE: 
YGL202W(ARO8)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0E00670(NCAS0E00670)
NDI: 
NDAI_0I02830(NDAI0I02830)
TPF: 
TPHA_0D03370(TPHA0D03370)
TDL: 
TDEL_0D05790(TDEL0D05790)
KAF: 
KAFR_0D01420(KAFR0D01420)
DHA: 
PIC: 
PGU: 
LEL: 
CAL: 
CTP: 
CDU: 
COT: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
MGR: 
FGR: 
NHE: 
TRE: 
VAL: 
SSL: 
BFU: 
ANI: 
NFI: 
AFM: 
AOR: 
AOR_1_454014(AO090026000245) AOR_1_786084(AO090020000444)
ANG: 
ANI_1_1292134(An15g02460) ANI_1_766024(An02g05540)
AFV: 
ACT: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
ZTR: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
LBC: 
SCM: 
DDI: 
DPP: 
DFA: 
ACAN: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
NGD: 
EHX: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:13366978]
  Authors
CANELLAKIS ZN, COHEN PP.
  Title
Purification studies of tyrosine-alpha-ketoglutaric acid transaminase.
  Journal
J. Biol. Chem. 222 (1956) 53-62.
  Organism
Canis familiaris
Reference
2  [PMID:13366979]
  Authors
CANELLAKIS ZN, COHEN PP.
  Title
Kinetic and substrate specificity study of tyrosine-alpha-ketoglutaric acid transaminase.
  Journal
J. Biol. Chem. 222 (1956) 63-71.
  Organism
Canis familiaris
Reference
3  [PMID:14171223]
  Authors
JACOBY GA, LADU BN.
  Title
STUDIES ON THE SPECIFICITY OF TYROSINE-ALPHA-KETOGLUTARATE TRANSAMINASE.
  Journal
J. Biol. Chem. 239 (1964) 419-24.
  Organism
Rattus norvegicus
Reference
4  [PMID:14408534]
  Authors
KENNEY FT.
  Title
Properties of partially purified tyrosine-alpha-ketoglutarate transaminase from rat liver.
  Journal
J. Biol. Chem. 234 (1959) 2707-12.
  Organism
Rattus norvegicus
Reference
5  [PMID:4396841]
  Authors
Miller JE, Litwack G.
  Title
Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase.
  Journal
J. Biol. Chem. 246 (1971) 3234-40.
  Organism
Rattus norvegicus
Reference
6  [PMID:13363833]
  Authors
ROWSELL EV.
  Title
Transaminations with L-glutamate and alpha-oxoglutarate in fresh extracts of animal tissues.
  Journal
Biochem. J. 64 (1956) 235-45.
  Organism
Sus scofa
Reference
7  [PMID:13750129]
  Authors
SENTHESHANMUGANATHAN S.
  Title
The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae.
  Journal
Biochem. J. 77 (1960) 619-25.
  Organism
Canis familiaris, Saccharomyces cerevisiae
Reference
8  [PMID:10074065]
  Authors
Heilbronn J, Wilson J, Berger BJ.
  Title
Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae.
  Journal
J. Bacteriol. 181 (1999) 1739-47.
  Organism
Klebsiella pneumoniae
  Sequence
[up:O85746]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9014-55-5

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