Promiscuous Yet Specific: A Methionine-Aromatic Interaction Drives the Reaction Scope of the Family 1 Glycosyltransferase GmUGT88E3 from Soybean.
Biochemistry
; 62(23): 3343-3346, 2023 12 05.
Article
in En
| MEDLINE
| ID: mdl-38009918
ABSTRACT
Family 1 glycosyltransferases (GT1s, UGTs) catalyze the regioselective glycosylation of natural products in a single step. We identified GmUGT88E3 as a particularly promising biocatalyst able to produce a variety of pure, single glycosidic products from polyphenols with high chemical yields. We investigated this particularly desirable duality toward specificity, i.e., promiscuous toward acceptors while regiospecific. Using high-field NMR, kinetic characterization, molecular dynamics simulations, and mutagenesis studies, we uncovered that the main molecular determinant of GmUGT88E3 specificity is a methionine-aromatic bridge, an interaction often present in protein structures but never reported for enzyme-substrate interactions. Here, mutating Met127 led to inactive proteins or 100-fold reduced activity.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Glycine max
/
Glycosyltransferases
Language:
En
Journal:
Biochemistry
Year:
2023
Document type:
Article
Affiliation country:
Denmark