Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1.

ABSTRACT: Glycosylation is a predominant strategy plants use to fine-tune the properties of small molecule metabolites to affect their bioactivity, transport, and storage. It is also important in biotechnology and medicine as many glycosides are utilized in human health. Small molecule glycosylation is largely carried out by family 1 glycosyltransferases. Here, we report a structural and biochemical investigation of UGT95A1, a family 1 GT enzyme from Pilosella officinarum that exhibits a strong, unusual regiospecificity for the 3'-O position of flavonoid acceptor substrate luteolin. We obtained an apo crystal structure to help drive the analyses of a series of binding site mutants, revealing that while most residues are tolerant to mutations, key residues M145 and D464 are important for overall glyc

SUBMITTER: Sirirungruang S 

PROVIDER: S-EPMC11381871 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature