Reaction participants Show >> << Hide
- Name help_outline L-tyrosine Identifier CHEBI:58315 Charge 0 Formula C9H11NO3 InChIKeyhelp_outline OUYCCCASQSFEME-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccc(O)cc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 53 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-dopa Identifier CHEBI:57504 Charge 0 Formula C9H11NO4 InChIKeyhelp_outline WTDRDQBEARUVNC-LURJTMIESA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccc(O)c(O)c1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:34283 | RHEA:34284 | RHEA:34285 | RHEA:34286 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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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.
The critical review describes the known dicopper systems mediating the aromatic hydroxylation of monophenolic substrates. Such systems are of interest as structural and functional models of the type 3 copper enzyme tyrosinase, which catalyzes the ortho-hydroxylation of tyrosine to DOPA and the sub ... >> More
The critical review describes the known dicopper systems mediating the aromatic hydroxylation of monophenolic substrates. Such systems are of interest as structural and functional models of the type 3 copper enzyme tyrosinase, which catalyzes the ortho-hydroxylation of tyrosine to DOPA and the subsequent two-electron oxidation to dopaquinone. Small-molecule systems involving μ-η²:η² peroxo, bis-μ-oxo and trans-μ-1,2 peroxo dicopper cores are considered separately. These tyrosinase models are contrasted to copper-dioxygen systems inducing radical reactions, and the different mechanistic pathways are discussed. In addition to considering the stoichiometric conversion of phenolic substrates, the available catalytic systems are described. The second part of the review deals with tyrosinase. After an introduction on the occurrence and function of tyrosinases, several aspects of the chemical reactivity of this class of enzymes are described. The analogies between the small-molecule and the enzymatic system are considered, and the implications for the reaction pathway of tyrosinase are discussed (140 references). << Less
Chem Soc Rev 40:4077-4098(2011) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Tyrosinase: a comprehensive review of its mechanism.
Sanchez-Ferrer A., Rodriguez-Lopez J.N., Garcia-Canovas F., Garcia-Carmona F.
Biochim Biophys Acta 1247:1-11(1995) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
RHEA:34283 part of RHEA:18117