Catalytic mechanism of tyrosinases.
Enzymes
; 56: 31-54, 2024.
Article
en En
| MEDLINE
| ID: mdl-39304290
ABSTRACT
Tyrosinases (TYR) play a key role in melanin biosynthesis by catalyzing two reactions monophenolase and diphenolase activities. Despite low amino acid sequence homology, TYRs from various organisms (from bacteria to humans) have similar active site architectures and catalytic mechanisms. The active site of the TYRs contains two copper ions coordinated by histidine (His) residues. The catalytic mechanism of TYRs involves electron transfer between copper sites, leading to the hydroxylation of monophenolic compounds to diphenols and the subsequent oxidation of these to corresponding dopaquinones. Although extensive studies have been conducted on the structure, catalytic mechanism, and enzymatic capabilities of TYRs, some mechanistic aspects are still debated. This chapter will delve into the structure of the active site, catalytic function, and inhibition mechanism of TYRs. The goal is to improve our understanding of the molecular mechanisms underlying TYR activity. This knowledge can help in developing new strategies to modulate TYR function and potentially treat diseases linked to melanin dysregulation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Monofenol Monooxigenasa
/
Dominio Catalítico
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Enzymes
Año:
2024
Tipo del documento:
Article