Radical formation on a conserved tyrosine residue is crucial for DyP activity.
Arch Biochem Biophys
; 537(2): 161-7, 2013 Sep 15.
Article
en En
| MEDLINE
| ID: mdl-23876237
Dye-decolorizing peroxidases (DyPs) are able to cleave bulky anthraquinone dyes. The recently published crystal structure of AauDyPI reveals that a direct oxidation in the distal heme cavity can be excluded for most DyP substrates. It is shown that a surface-exposed tyrosine residue acts as a substrate interaction site for bulky substrates. This amino acid is conserved in eucaryotic DyPs but is missing in the structurally related chlorite dismutases (Clds). Dye-decolorizing peroxidases of procaryotic origin equally possess a conserved tyrosine in the same region of the polypeptide albeit not at the homologous position.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Peroxidasas
/
Tirosina
/
Antraquinonas
/
Colorantes
Idioma:
En
Revista:
Arch Biochem Biophys
Año:
2013
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Estados Unidos