Structure, function and application of serine carboxypeptidase-like acyltransferases from plants.

Yu Wang; Yan Yang; Minzhi Liu; Wei Wang

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Structure, function and application of serine carboxypeptidase-like acyltransferases from plants.

Author: Yu WANG ¹ ; Yan YANG ¹ ; Minzhi LIU ¹ ; Wei WANG ¹
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1. State Key Laboratory of Bioactive and Function of Natural Medicines & Key Laboratory of Biosynthesis of Natural Products of National Health Commission of the People's Republic of China, Institute of Materia Medica, Chinese Academy of Medical Science and Peking Union Medical College, Beijing 100050, China.
Publication Type:Review
Keywords: acylation; bifunctional acyl and glucosyl donor; biocatalysis; serine carboxypeptidase-like acyltransferase
MeSH: Acylation; Acyltransferases/metabolism*; Carboxypeptidases/metabolism*; Plants/enzymology*
From: Chinese Journal of Biotechnology 2021;37(6):1887-1899
CountryChina
Language:Chinese
Abstract: Plant serine carboxypeptidase-like acyltransferases (SCPL-AT) have similar structural characteristics and high homology compared to the serine carboxypeptidase. They can transfer the acyl from acyl glucose esters to many natural products, participate in the acylation modification of plant secondary metabolites, enrich the structural diversity of natural products, and improve the physicochemical properties such as water solubility and stability of compounds. This review summarizes the structural characteristics, catalytic mechanism, functional characterization, and biocatalytic applications of SCPL-AT from plants. This will help to promote the functional characterization of these acyltransferase genes and the biosynthesis of useful plant secondary metabolites by synthetic biotechnology.