EC number:1.14.18.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.18.1 | ||
|---|---|---|---|
| Description: | Tyrosinase. | ||
| Alternative Name: |
Tyrosine-dopa oxidase. Phenolase. N-acetyl-6-hydroxytryptophan oxidase. Monophenol oxidase. Monophenol monooxygenase. Cresolase. | ||
| Prosite: | PDOC00398; | ||
| PDB: |
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| Cath: | 1.10.1280.10; 1.20.1370.10; 2.60.40.1520; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.18.1 |
| BRENDA Enzyme Link: | BRENDA 1.14.18.1 |
| KEGG Enzyme Link: | KEGG1.14.18.1 |
| BioCyc Enzyme Link: | BioCyc 1.14.18.1 |
| ExPASy Enzyme Link: | ExPASy1.14.18.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.18.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.18.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.18.1 |
| IntEnz Enzyme Link: | IntEnz 1.14.18.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.18.1 |
EC number:1.14.18.1
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:34287 | 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[c;H0;+0:4](-[OH;+0:5]):[c;H0;+0:6](-[OH;+0:7]):[cH;+0:8]:[cH;+0:9]:1.[*:10]-[c;H0;+0:11]1:[cH;+0:12]:[cH;+0:13]:[c;H0;+0:14](-[OH;+0:15]):[c;H0;+0:16](-[OH;+0:17]):[cH;+0:18]:1.[O;H0;+0:19]=[O;H0;+0:20]>>[*:1]-[C;H0;+0:2]1=[CH;+0:3]-[C;H0;+0:4](=[O;H0;+0:5])-[C;H0;+0:6](=[O;H0;+0:7])-[CH;+0:8]=[CH;+0:9]-1.[*:10]-[C;H0;+0:11]1=[CH;+0:18]-[C;H0;+0:16](=[O;H0;+0:17])-[C;H0;+0:14](=[O;H0;+0:15])-[CH;+0:13]=[CH;+0:12]-1.[OH2;+0:19].[OH2;+0:20] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Tyrosinase: a comprehensive review of its mechanism. | Sánchez-Ferrer A, Rodríguez-López JN, García-Cánovas F, García-Carmona F | 1995 Feb 22 | 7873577 |
| Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. | Rolff M, Schottenheim J, Decker H, Tuczek F | 2011 Jul | 21416076 |
| Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko. | Kawamura-Konishi Y, Tsuji M, Hatana S, Asanuma M, Kakuta D, Kawano T, Mukouyama EB, Goto H, Suzuki H | 2007 Jul | 17617709 |
| RHEA:18117 | L-tyrosine + O2 = H2O + L-dopaquinone |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[cH;+0:4]:[c;H0;+0:5](-[OH;+0:6]):[cH;+0:7]:[cH;+0:8]:1.[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[C;H0;+0:2]1=[CH;+0:8]-[C;H0;+0:7](=[O;H0;+0:10])-[C;H0;+0:5](=[O;H0;+0:6])-[CH;+0:4]=[CH;+0:3]-1.[OH2;+0:9] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures. | Steiner U, Schliemann W, Strack D | 1996 Jun 15 | 8660589 |
| Tyrosinase: a comprehensive review of its mechanism. | Sánchez-Ferrer A, Rodríguez-López JN, García-Cánovas F, García-Carmona F | 1995 Feb 22 | 7873577 |
| Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. | Rolff M, Schottenheim J, Decker H, Tuczek F | 2011 Jul | 21416076 |
| Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko. | Kawamura-Konishi Y, Tsuji M, Hatana S, Asanuma M, Kakuta D, Kawano T, Mukouyama EB, Goto H, Suzuki H | 2007 Jul | 17617709 |