ENZYME entry: EC 1.10.3.1
| Accepted Name |
| Catechol oxidase.
|
| Alternative Name(s) |
| Diphenol oxidase. |
| o-diphenolase. |
| Phenolase. |
| Polyphenol oxidase. |
| Tyrosinase. |
| Reaction catalysed |
| 2 catechol + O(2) <=> 2 1,2-benzoquinone + 2 H(2)O |
| Cofactor(s) |
| Copper.
|
| Comment(s) |
- Also acts on a variety of substituted catechols.
- Many of these enzymes also catalyze the reaction listed under
EC 1.14.18.1; this is especially true for the classical tyrosinase.
|
| Cross-references |
| PROSITE | PDOC00398 |
| BRENDA | 1.10.3.1 |
| EC2PDB | 1.10.3.1 |
| ExplorEnz | 1.10.3.1 |
| PRIAM enzyme-specific profiles | 1.10.3.1 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.10.3.1 |
| IUBMB Enzyme Nomenclature | 1.10.3.1 |
| IntEnz | 1.10.3.1 |
| MEDLINE | Find literature relating to 1.10.3.1 |
| MetaCyc | 1.10.3.1 |
| UniProtKB/Swiss-Prot |
| Q00024, PPO1_AGABI; | Q9ZP19, PPO1_IPOBA; | Q9MB14, PPO2_IPOBA; |
| Q08303, PPOA_SOLLC; | Q08304, PPOB_SOLLC; | Q06355, PPOB_SOLTU; |
| Q08305, PPOC_SOLLC; | Q08306, PPOD_SOLLC; | Q08307, PPOE_SOLLC; |
| Q08296, PPOF_SOLLC; | P43309, PPO_MALDO; | P43310, PPO_SPIOL; |
| Q06215, PPO_VICFA; | P43311, PPO_VITVI; | P85026, PPO_ZINOF; |
|
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