Plant-specific type III polyketide synthases superfamily: crystal structures and functions.
- Author:
Heshu LÜ
1
;
Chunmei LIU
;
Ping LU
;
Guanglu SHI
;
Lanqing MA
;
Younian WANG
Author Information
1. Key Laboratory of Urban Agriculture North) of Ministry of Agriculture China, Beijing University of Agriculture, Beijing 102206, China.
- Publication Type:Journal Article
- MeSH:
Acyltransferases;
chemistry;
genetics;
physiology;
Amino Acid Sequence;
Catalysis;
Chalcones;
Crystallization;
Flavanones;
Genetic Engineering;
Metabolic Engineering;
Molecular Sequence Data;
Plant Proteins;
chemistry;
genetics;
physiology;
Plants;
enzymology;
genetics;
Protein Structure, Secondary;
Substrate Specificity
- From:
Chinese Journal of Biotechnology
2012;28(1):1-14
- CountryChina
- Language:Chinese
-
Abstract:
Plant type III polyketide synthase (PKS) generates backbones of a variety of plant secondary metabolites with diverse functions, and has long been models to elucidate the relationship between the three-dimensional structure and function. More than 80 type IIII PKS crystal structures with different functions have been reported in Protein Data Bank, including the crystal structures of the well-studied Chalcone Synthase of plant type III PKS, as well as the 6 other kinds of PKSs in the family, which are critical for understanding the structural basis for diverse starter molecule selectivity, polyketide chain length and the cyclization reaction. Structure-based analysis and site-directed mutagenesis are foundation for the investigation of enzyme engineering, genetic and metabolic engineering. This review summarized 7 plant-specific type III PKS in the aspects of their crystal structures and functions.