Beyond Phenolics: Alternative Substrates for Type III Copper Enzymes

Abstract: The type III copper enzyme family of tyrosinases (TYRs) catalyzes the ortho‐hydroxylation and oxidation of phenols as well as the two‐electron oxidation of catechols to ortho‐quinones. TYRs use copper ions as their tightly bound cofactors and utilize molecular oxygen as their cosubstrate. They are responsible for physiologically important reactions like the formation of melanin, the primary pigment animals apply for protection against UV light. While the reactivity of TYRs on substrates containing aromatic hydroxy groups (i. e. phenols) is well recognized, reports clearly demonstrating that TYRs are active on aromatic amines as well have gone largely unnoticed. In this perspective we aim to bring together the sparse data on non‐phenolic TYR substrates to illustrate the potential of TYRs for the oxidation of aminophenols and anilines. The activity of TYRs on aromatic amines extends the substance classes amenable to biotechnological production with TYRs from catechols to N‐phenyl imines and phenoxazinone derivates and calls for the inclusion of TYRs among the candidates for oxidative modification of aromatic amines in metabolic pathways.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Beyond Phenolics: Alternative Substrates for Type III Copper Enzymes ; day:18 ; month:02 ; year:2025 ; extent:8
ChemBioChem ; (18.02.2025) (gesamt 8)

Creator
Pretzler, Matthias
Rompel, Annette

DOI
10.1002/cbic.202400982
URN
urn:nbn:de:101:1-2502181329335.734251646498
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:46 AM CEST

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