Molecular basis of ligand recognition specificity of flavone glucosyltransferases in Nemophila menziesii.
Arch Biochem Biophys
; 753: 109926, 2024 03.
Article
en En
| MEDLINE
| ID: mdl-38346547
ABSTRACT
Of the more than 100 families of glycosyltransferases, family 1 glycosyltransferases catalyze glycosylation using uridine diphosphate (UDP)-sugar as a sugar donor and are thus referred to as UDP-sugarglycosyl transferases. The blue color of the Nemophila menziesii flower is derived from metalloanthocyanin, which consists of anthocyanin, flavone, and metal ions. Flavone 7-O-ß-glucoside-4'-O-ß-glucoside in the plant is sequentially biosynthesized from flavons by UDP-glucoseflavone 4'-O-glucosyltransferase (NmF4'GT) and UDP-glucoseflavone 4'-O-glucoside 7-O-glucosyltransferase (NmF4'G7GT). To identify the molecular mechanisms of glucosylation of flavone, the crystal structures of NmF4'G7GT in its apo form and in complex with UDP-glucose or luteolin were determined, and molecular structure prediction using AlphaFold2 was conducted for NmF4'GT. The crystal structures revealed that the size of the ligand-binding pocket and interaction environment for the glucose moiety at the pocket entrance plays a critical role in the substrate preference in NmF4'G7GT. The substrate specificity of NmF4'GT was examined by comparing its model structure with that of NmF4'G7GT. The structure of NmF4'GT may have a smaller acceptor pocket, leading to a substrate preference for non-glucosylated flavones (or flavone aglycones).
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Flavonas
/
Glucosiltransferasas
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Arch Biochem Biophys
Año:
2024
Tipo del documento:
Article
País de afiliación:
Japón