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].
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)
MMU: 
234724(Tat)
RNO: 
24813(Tat)
CFA: 
479665(TAT)
AML: 
FCA: 
101080599(TAT)
BTA: 
533481(TAT)
SSC: 
100511756(TAT)
ECB: 
100068116(TAT)
MDO: 
100020832(TAT)
SHR: 
100925059(TAT)
OAA: 
100077699(TAT)
GGA: 
415884(TAT)
MGP: 
100549583(TAT)
TGU: 
100230394(TAT)
ACS: 
100559092
XTR: 
448486(tat)
DRE: 
561410(tat)
TRU: 
101067692
OLA: 
101171329
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
DWI: 
Dwil_GK20156
DYA: 
Dyak_GE17134
DGR: 
Dgri_GH12929
DMO: 
Dmoj_GI15439
DVI: 
Dvir_GJ19064
AGA: 
AgaP_AGAP000327
AAG: 
AaeL_AAEL008963
CQU: 
CpipJ_CPIJ003774
AME: 
725204
NVI: 
100119866(NV11108)
TCA: 
659321
PHU: 
Phum_PHUM509510
ISC: 
IscW_ISCW014463
CEL: 
CELE_F42D1.2(tatn-1)
CBR: 
CBG07591
BMY: 
Bm1_31005
NVE: 
NEMVE_v1g207788
HMG: 
100204677
TAD: 
TRIADDRAFT_35383
AQU: 
100635686
ATH: 
AT2G24850(TAT3) AT4G23590 AT4G23600(CORI3) AT4G28410 AT4G28420 AT5G36160 AT5G53970
ALY: 
ARALYDRAFT_481345 ARALYDRAFT_491928 ARALYDRAFT_492508 ARALYDRAFT_493655 ARALYDRAFT_914237 ARALYDRAFT_918507
GMX: 
100784392 100785132 100787587 100800297 100800830 732650
MTR: 
MTR_8g061360
CSV: 
101212407 101221092 101229685 101231189
RCU: 
RCOM_0651460 RCOM_1173030 RCOM_1173140
POP: 
POPTR_562159(AMT8) POPTR_562160(AMT9) POPTR_562161(AMT10) POPTR_568851(AMT7) POPTR_582454(AMT3) POPTR_594645(AMT6) POPTR_594647(AMT2) POPTR_672102(AMT5) POPTR_680943(AMT4) POPTR_836654(AMT1)
VVI: 
100241782 100242005 100247148 100253895 100259032
OSA: 
4329098 4329101 4340970 4350712 4351017
DOSA: 
Os02t0302200-01(Os02g0302200) Os02t0302700-01(Os02g0302700) Os02t0306401-00(Os02g0306401) Os06t0345200-02(Os06g0345200) Os11t0552000-01(Os11g0552000) Os11t0644800-00(Os11g0644800)
BDI: 
100822209 100825535 100828620 100831451 100841166
SBI: 
SORBI_02g003520(SORBIDRAFT_02g003520) SORBI_03g026220(SORBIDRAFT_03g026220) SORBI_05g021600(SORBIDRAFT_05g021600) SORBI_05g021610(SORBIDRAFT_05g021610) SORBI_08g000600(SORBIDRAFT_08g000600)
ZMA: 
100191283(pco115235a) 100191816 100193424 100279205 100279999
SMO: 
SELMODRAFT_139117
PPP: 
PHYPADRAFT_215944
OLU: 
OSTLU_3820
OTA: 
Ot01g04390
CME: 
CMT533C
SCE: 
YGL202W(ARO8)
AGO: 
AGOS_AFR548C
ERC: 
Ecym_7228
KLA: 
KLLA0F10021g
LTH: 
KLTH0G02002g
PPA: 
PAS_chr1-4_0608
VPO: 
Kpol_278p2
ZRO: 
ZYRO0C06028g
CGR: 
CAGL0G01254g
NCS: 
NCAS_0E00670(NCAS0E00670)
NDI: 
NDAI_0I02830(NDAI0I02830)
TPF: 
TPHA_0D03370(TPHA0D03370)
TDL: 
TDEL_0D05790(TDEL0D05790)
KAF: 
KAFR_0D01420(KAFR0D01420)
DHA: 
DEHA2A06886g
PIC: 
PICST_66767(ARO8)
PGU: 
PGUG_02078 PGUG_04621
LEL: 
LELG_01198
CAL: 
CaO19.2098(ARO8) CaO19.9645(ARO8)
CTP: 
CTRG_01079
CDU: 
CD36_15310
COT: 
CORT_0A12760
YLI: 
YALI0E20977g
CLU: 
CLUG_00783
NCR: 
NCU09116
SMP: 
SMAC_04612
PAN: 
PODANSg5646
TTT: 
THITE_2121569
MTM: 
MYCTH_2294749
MGR: 
MGG_09919
FGR: 
FG01285.1
NHE: 
NECHADRAFT_51829 NECHADRAFT_74483
VAL: 
VDBG_04940
SSL: 
SS1G_10035
BFU: 
BC1G_07219
ANI: 
AN6338.2
NFI: 
NFIA_088830
AFM: 
AFUA_2G13630
AOR: 
AOR_1_454014(AO090026000245)
ANG: 
ANI_1_766024(An02g05540)
AFV: 
AFLA_099700 AFLA_136830
ACT: 
ACLA_073980
PCS: 
Pc12g11860
CIM: 
CIMG_04628
CPW: 
CPC735_071790
PBL: 
PAAG_05743
URE: 
UREG_01826
ABE: 
ARB_01306
TVE: 
TRV_00012
AJE: 
HCAG_04617
PNO: 
SNOG_04259
PTE: 
PTT_08476
ZTR: 
MYCGRDRAFT_100367
TML: 
GSTUM_00008805001
SPO: 
SPAC56E4.03 SPBC1773.13 SPCC569.07
CNE: 
CNF04620
CNB: 
CNBB2510 CNBF0280
CGI: 
CGB_A3370W
LBC: 
LACBIDRAFT_311755
SCM: 
SCHCODRAFT_105805 SCHCODRAFT_15733 SCHCODRAFT_62391 SCHCODRAFT_80399
NGR: 
NAEGRDRAFT_56385
DDI: 
DDB_G0287515(tat)
DPP: 
DICPUDRAFT_32147
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: 
LMJF_36_2360(TAT)
LIF: 
LINJ_36_2490(TAT)
LDO: 
LDBPK_362490
LMI: 
LMXM_36_2360
LBZ: 
LBRM_35_2580(TAT)
PTI: 
PHATR_51609
TPS: 
THAPSDRAFT_268594
PIF: 
PITG_03427
 » 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 [GN:cfa]
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 [GN:cfa]
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 [GN:rno]
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 [GN:rno]
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 [GN:rno]
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 [GN:ssc]
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 [GN:cfa], Saccharomyces cerevisiae [GN:sce]
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 [GN:kpn]
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
DBGET integrated database retrieval system