Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.
Biotechnol Lett
; 36(3): 633-9, 2014 Mar.
Article
en En
| MEDLINE
| ID: mdl-24338160
The shape of the hydrophobic tunnel leading to the active site of Penicillium expansum lipase (PEL) was redesigned by single-point mutations, in order to better understand enzyme enantioselectivity towards naproxen. A variant with a valine-to-glycine substitution at residue 237 exhibited almost no enantioselectivity (E = 1.1) compared with that (E = 104) of wild-type PEL. The function of the residue, Val237, in the hydrophobic tunnel was further analyzed by site-directed mutagenesis. For each of these variants a significant decrease of enantioselectivity (E < 7) was observed compared with that of wild-type enzyme. Further docking result showed that Val237 plays the most important role in stabilizing the correct orientation of (R)-naproxen. Overall, these results indicate that the residue Val237 is the key amino acid residue maintaining the enantioselectivity of the lipase.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Penicillium
/
Valina
/
Naproxeno
/
Lipasa
Idioma:
En
Revista:
Biotechnol Lett
Año:
2014
Tipo del documento:
Article
Pais de publicación:
Países Bajos