Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin.
Angew Chem Int Ed Engl
; 57(20): 5823-5827, 2018 05 14.
Article
en En
| MEDLINE
| ID: mdl-29536601
ABSTRACT
Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report high-resolution X-ray crystal structures of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase (SpnD-AT) in the apo form and in complex with benzylmalonyl and pentynylmalonyl extender unit mimics. These structures revealed the molecular basis for the stereoselectivity and substrate specificity of SpnD-AT, and enabled the engineering of the industrially important Ery-AT6 to broaden its substrate scope to include three new types of extender units.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Aciltransferasas
/
Sintasas Poliquetidas
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2018
Tipo del documento:
Article
País de afiliación:
China