Deactivating mutations in the catalytic site of a companion serine carboxypeptidase-like acyltransferase enhance catechin galloylation in <i>Camellia</i> plants.

ABSTRACT: Galloylated flavan-3-ols are key quality and health-related compounds in tea plants of Camellia section Thea. Camellia ptilophylla and Camellia sinensis are two representative species known for their high levels of galloylated flavan-3-ols. Building on our knowledge of galloyl catechin biosynthesis in C. sinensis, we now focus on the biosynthesis of galloylated phenolics in C. ptilophylla, aiming to elucidate the mechanisms underlying the high accumulation of these compounds in Camellia species. The phenolic compounds in C. ptilophylla were identified and quantified using chromatographic and colorimetric methods. Genes involved in polyphenol galloylation were identified by correlating gene expression with the accumulation of galloylat

SUBMITTER: Chen X 

PROVIDER: S-EPMC11886809 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature