KEGG   ENZYME: 1.14.18.1Help
Entry
EC 1.14.18.1                Enzyme                                 

Name
tyrosinase;
monophenol monooxygenase;
phenolase;
monophenol oxidase;
cresolase;
monophenolase;
tyrosine-dopa oxidase;
monophenol monooxidase;
monophenol dihydroxyphenylalanine:oxygen oxidoreductase;
N-acetyl-6-hydroxytryptophan oxidase;
monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase;
o-diphenol:O2 oxidoreductase;
phenol oxidase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With another compound as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
L-tyrosine,L-dopa:oxygen oxidoreductase
Reaction(IUBMB)
(1) L-tyrosine + O2 = dopaquinone + H2O (overall reaction);
(1a) L-tyrosine + 1/2 O2 = L-dopa [RN:R00031];
(1b) L-dopa + 1/2 O2 = dopaquinone + H2O;
(2) 2 L-dopa + O2 = 2 dopaquinone + 2 H2O [RN:R00045]
Reaction(KEGG)
Substrate
L-tyrosine [CPD:C00082];
O2 [CPD:C00007];
L-dopa [CPD:C00355]
Product
dopaquinone [CPD:C00822];
H2O [CPD:C00001];
L-dopa [CPD:C00355]
Comment
A type III copper protein found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin. The enzyme, which is activated upon binding molecular oxygen, can catalyse both a monophenolase reaction cycle (reaction 1) or a diphenolase reaction cycle (reaction 2). During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an o-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule. The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule. During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an o-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state. The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state [7]. The second reaction is identical to that catalysed by the related enzyme catechol oxidase (EC 1.10.3.1). However, the latter can not catalyse the hydroxylation or monooxygenation of monophenols.
History
EC 1.14.18.1 created 1972, modified 1976, modified 1980 (EC 1.14.17.2 created 1972, incorporated 1984), modified 2012
Pathway
ec00350  Tyrosine metabolism
ec00950  Isoquinoline alkaloid biosynthesis
ec00965  Betalain biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00505  tyrosinase
Genes
HSA: 7299(TYR)
PTR: 451473(TYR)
PPS: 100989128(TYR)
GGO: 101148846(TYR)
PON: 100453479(TYR)
NLE: 100594055(TYR)
MCC: 705792(TYR)
MCF: 102141480(TYR)
CSAB: 103248194(TYR)
RRO: 104657434(TYR)
RBB: 108539149(TYR)
CJC: 100399713(TYR)
SBQ: 101043674(TYR)
MMU: 22173(Tyr)
RNO: 308800(Tyr)
CGE: 100752294(Tyr)
NGI: 103743041(Tyr) 103750541
HGL: 101696609(Tyr)
OCU: 100008753(TYR)
TUP: 102485831(TYR)
CFA: 403405(TYR)
AML: 100475022(TYR)
UMR: 103675370(TYR)
ORO: 101363864(TYR)
FCA: 751100(TYR)
PTG: 102957473(TYR)
AJU: 106967790(TYR)
BTA: 280951(TYR)
BOM: 102272000(TYR)
BIU: 109554196(TYR)
PHD: 102324178(TYR)
CHX: 102182281(TYR)
OAS: 780502(TYR)
SSC: 407745(TYR)
CFR: 102509800(TYR)
CDK: 105088592(TYR)
BACU: 103016545(TYR)
OOR: 101280655(TYR)
ECB: 100060227(TYR)
EPZ: 103547855(TYR)
EAI: 106822679(TYR)
MYB: 102260258(TYR)
MYD: 102762530(TYR)
HAI: 109374039(TYR)
RSS: 109451381(TYR)
PALE: 102894376(TYR)
LAV: 100676924(TYR)
TMU: 101358815
MDO: 100010166(TYR)
SHR: 100928294 100934956(TYR)
OAA: 100080574(TYR)
GGA: 373971(TYR)
MGP: 100538462(TYR)
CJO: 107308457(TYR)
APLA: 101791683(TYR)
ACYG: 106034185(TYR)
TGU: 100225893(TYR)
GFR: 102035437(TYR)
FAB: 101814779(TYR)
PHI: 102104800(TYR)
PMAJ: 107199861(TYR)
CCAE: 111924932(TYR)
CCW: 104690323(TYR)
FPG: 101915664(TYR)
FCH: 102054260(TYR)
CLV: 102093703(TYR)
EGZ: 104128835(TYR)
AAM: 106495505(TYR)
ASN: 102385049(TYR)
AMJ: 102560883(TYR)
PSS: 102454532(TYR)
CMY: 102935011(TYR)
CPIC: 101935010(TYR)
ACS: 100552257(tyr)
PVT: 110088582(TYR)
PBI: 103060005(TYR) 103063605
GJA: 107119489(TYR)
XTR: 100125152(tyr)
DRE: 30207(tyr)
SGH: 107558837(tyr)
TRU: 101064772(tyr) 101080145
LCO: 104920119(tyr)
NCC: 104963013(tyr)
OLA: 100049427(tyr) 101171514
XMA: 102216777 102222951(tyr)
PRET: 103474486(tyr) 103475522
NFU: 107380455(tyr) 107386962
KMR: 108236980 108244618(tyr)
CSEM: 103378543(tyr) 103395402
HCQ: 109509733 109525374(tyr)
BPEC: 110158560 110174305(tyr)
MALB: 109959313 109971605(tyr)
ELS: 105024066(tyr) 105026640
SFM: 108923732 108932465(tyr)
LCM: 102365572(TYR)
CMK: 103174506 103185187(tyr)
DME: Dmel_CG42639(PPO1) Dmel_CG42640(PPO3)
DSI: Dsimw501_GD11733(Dsim_GD11733)
TUT: 107369608
CEL: CELE_C34G6.2(tyr-4)
CBR: CBG04025(Cbr-tyr-4)
NTE: NEUTE1DRAFT103253(NEUTE1DRAFT_103253) NEUTE1DRAFT117718(NEUTE1DRAFT_117718) NEUTE1DRAFT118745(NEUTE1DRAFT_118745) NEUTE1DRAFT124197(NEUTE1DRAFT_124197) NEUTE1DRAFT125579(NEUTE1DRAFT_125579) NEUTE1DRAFT93419(NEUTE1DRAFT_93419)
ANG: ANI_1_1250014(An01g09220) ANI_1_1268084(An09g02980) ANI_1_1436104(An12g01670) ANI_1_1454084(An09g05130) ANI_1_1798134(An15g07670) ANI_1_26034(An03g00280)
ABE: ARB_00532
TVE: TRV_00392
ABP: AGABI1DRAFT114468(AGABI1DRAFT_114468) AGABI1DRAFT114491(AGABI1DRAFT_114491) AGABI1DRAFT114493(AGABI1DRAFT_114493) AGABI1DRAFT116717(AGABI1DRAFT_116717) AGABI1DRAFT62737(AGABI1DRAFT_62737) AGABI1DRAFT85838(AGABI1DRAFT_85838)
ABV: AGABI2DRAFT135027(AGABI2DRAFT_135027) AGABI2DRAFT191507(AGABI2DRAFT_191507) AGABI2DRAFT191532(AGABI2DRAFT_191532) AGABI2DRAFT194055(AGABI2DRAFT_194055) AGABI2DRAFT239416(AGABI2DRAFT_239416)
PTI: PHATRDRAFT_40017(TYR1)
LEM: LEN_2997(melC2)
PPT: PPS_2676
PPUH: B479_12930
PPUN: PP4_19320
PPUD: DW66_2934
PMON: X969_12705
PMOT: X970_12350
PFO: Pfl01_3461(melC2)
PFC: PflA506_4965(melC2)
PFB: VO64_2552
PSIL: PMA3_28020
HCH: HCH_03392
CVI: CV_3262
BPS: BPSS1731
BPSE: BDL_5087(melO)
BPSM: BBQ_4408(melO)
BPSU: BBN_5187(melO)
BPSD: BBX_4253(melO)
BPK: BBK_4451(melO)
BPSH: DR55_3536(melO)
BPSA: BBU_4293(melO)
BPSO: X996_5813(melO)
BUT: X994_5374(melO)
BTQ: BTQ_3941(melO)
BTJ: BTJ_4973(melO)
BTZ: BTL_3442(melO)
BTD: BTI_3837
BTV: BTHA_4444(melO)
BTHE: BTN_5428(melO)
BTHM: BTRA_5703(melO)
BTHA: DR62_5606
BTHL: BG87_3396(melO)
BOK: DM82_4935(melC2) DM82_5976(melO)
BOC: BG90_4662(melO) BG90_5660(melC2)
BCON: NL30_37765
BUB: BW23_4486(melO) BW23_6019
BSTG: WT74_18825
BUL: BW21_5830
BPH: Bphy_4746
NEU: NE1241
SMX: SM11_pC0105(mepA1)
RHN: AMJ98_PC00117(melA)
AOL: S58_42440
RPB: RPB_2167
NWI: Nwi_0968
MET: M446_5336
MSC: BN69_0277
PDE: Pden_4643
MALG: MALG_04738
RSU: NHU_02308
TXI: TH3_18755
BCA: BCE_A0211
BMQ: BMQ_3385
BMD: BMD_3389
BMH: BMWSH_1797(melC1)
BMEG: BG04_300(melC2)
BEO: BEH_25025
CEF: CE1756
SCO: SCO2700(melC2)
SMA: SAVERM_1137(melC2) SAVERM_5362(melC2-2)
SGR: SGR_2447(melC2-2) SGR_527(melC2-1)
SGB: WQO_32205
SCB: SCAB_59241(melC2) SCAB_85681(melC2B)
SFA: Sfla_5963
SHY: SHJG_4198
SDV: BN159_5596(melC2) BN159_7561 BN159_8269(melC2)
STRP: F750_0607
SFI: SFUL_6847
SLV: SLIV_24170(melC2)
SAMB: SAM23877_2730(melC)
SPRI: SPRI_2876
SRW: TUE45_00932(melC2_1) TUE45_03314(melC2_2)
SLE: sle_45350(sle_45350)
SRN: A4G23_03056(melC2)
STRD: NI25_25425
SLAU: SLA_4839
SLX: SLAV_04435(melC1) SLAV_04520(melC2) SLAV_32845(melC3) SLAV_35305(melC4)
SFK: KY5_2844c
FAL: FRAAL0531
SESP: BN6_45030(melC2)
ASE: ACPL_5017(griF)
ACTS: ACWT_4887
RXY: Rxyl_1947
AMR: AM1_B0356
CTHE: Chro_3115
SACI: Sinac_0162
SUS: Acid_5081
ABAC: LuPra_02564(melC2)
FLN: FLA_2632
DFE: Dfer_1836
CBAL: M667_12305
CBAT: M666_12215
KOS: KORDIASMS9_02290(melC2)
TAA: NMY3_00348(griF) NMY3_03193(melC2)
 » show all
Taxonomy
Reference
1
  Authors
Dawson, C.R. and Tarpley, W.B.
  Title
The copper oxidases.
  Journal
In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, 1st ed., vol. 2, Academic Press, New York, 1951, p. 454-498.
Reference
2  [PMID:5842066]
  Authors
Patil SS, Zucker M.
  Title
Potato phenolases. Purification and properties.
  Journal
J Biol Chem 240:3938-43 (1965)
Reference
3  [PMID:13972077]
  Authors
POMERANTZ SH.
  Title
Separation, purification, and properties of two tyrosinases from hamster melanoma.
  Journal
J Biol Chem 238:2351-7 (1963)
Reference
4
  Authors
Robb, D.A.
  Title
`Tyrosinase.
  Journal
In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, p. 207-240.
Reference
5  [PMID:7873577]
  Authors
Sanchez-Ferrer A, Rodriguez-Lopez JN, Garcia-Canovas F, Garcia-Carmona F
  Title
Tyrosinase: a comprehensive review of its mechanism.
  Journal
Biochim Biophys Acta 1247:1-11 (1995)
DOI:10.1016/0167-4838(94)00204-T
Reference
6  [PMID:8660589]
  Authors
Steiner U, Schliemann W, Strack D
  Title
Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures.
  Journal
Anal Biochem 238:72-5 (1996)
DOI:10.1006/abio.1996.0253
Reference
7  [PMID:21416076]
  Authors
Rolff M, Schottenheim J, Decker H, Tuczek F
  Title
Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme.
  Journal
Chem Soc Rev 40:4077-98 (2011)
DOI:10.1039/c0cs00202j
Other DBs
ExplorEnz - The Enzyme Database: 1.14.18.1
IUBMB Enzyme Nomenclature: 1.14.18.1
ExPASy - ENZYME nomenclature database: 1.14.18.1
BRENDA, the Enzyme Database: 1.14.18.1
CAS: 9002-10-2

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