A dynamic understanding of cytochrome P450 structure and function through solution NMR.
Curr Opin Biotechnol
; 69: 35-42, 2021 06.
Article
en En
| MEDLINE
| ID: mdl-33360373
ABSTRACT
Many economically important biosyntheses incorporate regiospecific and stereospecific oxidations at unactivated carbons. Such oxidations are commonly catalyzed by cytochrome P450 monooxygenases, heme-containing enzymes that activate molecular oxygen while selectively binding and orienting the substrate for reaction. Despite the plethora of P450-catalyzed reactions, the P450 fold is highly conserved, and static structures are often insufficient for characterizing conformational states that contribute to specificity. High-resolution solution nuclear magnetic resonance (NMR) offers insights into dynamic processes and conformational changes that are required of a P450 in order to attain the combination of specificity and efficiency required for these reactions.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Sistema Enzimático del Citocromo P-450
Idioma:
En
Revista:
Curr Opin Biotechnol
Asunto de la revista:
BIOTECNOLOGIA
Año:
2021
Tipo del documento:
Article