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 [RN:R00045];
(2) 2 L-dopa + O2 = 2 dopaquinone + 2 H2O
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
Tyrosine metabolism
Riboflavin metabolism
Isoquinoline alkaloid biosynthesis
Betalain biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00505  
tyrosinase
Genes
HSA: 
7299(TYR)
PTR: 
451473(TYR)
PPS: 
GGO: 
PON: 
MCC: 
705792(TYR)
MCF: 
MMU: 
22173(Tyr)
RNO: 
308800(Tyr)
CGE: 
HGL: 
TUP: 
CFA: 
403405(TYR)
AML: 
FCA: 
751100(TYR)
PTG: 
BTA: 
280951(TYR)
BOM: 
PHD: 
CHX: 
OAS: 
780502(TYR)
SSC: 
407745(TYR)
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
373971(TYR)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XTR: 
DRE: 
30207(tyr)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
DME: 
Dmel_CG42639(proPO-A1) Dmel_CG42640(proPO59)
DPO: 
DER: 
Dere_GG22822(Dere_Dox-A3)
DSI: 
DYA: 
CEL: 
CBR: 
CBG04025(Cbr-tyr-4)
LOA: 
SMM: 
CVR: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_1028194(AO090012000590) AOR_1_278014(AO090026000145) AOR_1_662164(AO090001000383) AOR_1_722144(AO090023000424) AOR_1_932024(AO090010000557)
ANG: 
ANI_1_1250014(An01g09220) ANI_1_1798134(An15g07670) ANI_1_26034(An03g00280)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
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)
CPUT: 
SLA: 
PFP: 
PGR: 
MLR: 
WSE: 
EIN: 
EHE: 
PTI: 
PIF: 
EHX: 
BUJ: 
VNI: 
PPUN: 
PFO: 
PFC: 
PCH: 
MME: 
CVI: 
RSO: 
RSc1501(mel)
RSC: 
RSL: 
RSN: 
RSM: 
RSE: 
BPS: 
BPM: 
BPL: 
BPD: 
BPSE: 
BDL_5087(melO)
BPSM: 
BBQ_4408(melO)
BPSU: 
BBN_5187(melO)
BPSD: 
BBX_4253(melO)
BPZ: 
BPQ: 
BPK: 
BBK_4451(melO)
BTE: 
BTQ: 
BTQ_3941(melO)
BTJ: 
BTJ_4973(melO)
BTZ: 
BTL_3442(melO)
BTD: 
BUR: 
BPH: 
JAG: 
NEU: 
NMU: 
SCU: 
MCI: 
MOP: 
MAM: 
SMX: 
RET: 
BJU: 
AOL: 
RPB: 
NWI: 
NHA: 
MET: 
MSC: 
ALI: 
BCA: 
BCU: 
BTB: 
BTHT: 
BMQ: 
BMD: 
BMH: 
BMWSH_1797(melC1)
CEF: 
SCO: 
SCO2700(melC2)
SMA: 
SAV_1137(melC1) SAV_5362(melC1-2)
SGR: 
SGR_2447(melC2-2) SGR_527(melC2-1)
SCB: 
SCAB_59241(melC2) SCAB_85681(melC2B)
SSX: 
SFA: 
SHY: 
SHO: 
SVE: 
SDV: 
STRP: 
SFI: 
SCI: 
SLV: 
SLIV_24170(melC2)
FRA: 
FRE: 
FAL: 
FSY: 
SESP: 
BN6_45030(melC2)
ASE: 
ACPL_5017(griF)
RXY: 
GMA: 
TSA: 
SUS: 
SACI: 
AMR: 
GLP: 
NPU: 
RIV: 
CTHE: 
DFE: 
CAO: 
FGI: 
NIR: 
NKR: 
 » 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 (1965) 3938-43.
Reference
3  [PMID:13972077]
  Authors
POMERANTZ SH.
  Title
Separation, purification, and properties of two tyrosinases from hamster melanoma.
  Journal
J. Biol. Chem. 238 (1963) 2351-7.
Reference
4  [PMID:13972077]
  Authors
POMERANTZ SH.
  Title
Separation, purification, and properties of two tyrosinases from hamster melanoma.
  Journal
J. Biol. Chem. 238 (1963) 2351-7.
Reference
5
  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
6
  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
7  [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 (1995) 1-11.
Reference
8  [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 (1995) 1-11.
Reference
9  [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 (1996) 72-5.
Reference
10 [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 (1996) 72-5.
Reference
11 [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 (2011) 4077-98.
Reference
12 [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 (2011) 4077-98.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9002-10-2

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