Open AccessOuter‐sphere residues influence the catalytic activity of a chalcone synthase from Polygonum cuspidatum
Author(s) -
Shen Yalin,
Li Xing,
Chai Tuanyao,
Wang Hong
Publication year - 2016
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12072
Subject(s) - chalcone synthase , enzyme , mutant , chalcone , chemistry , atp synthase , biochemistry , enzyme assay , stereochemistry , transferase , biosynthesis , gene
We have previously cloned a chalcone synthase (Pc CHS 1) from Polygonum cuspidatum and biochemically identified its enzymatic dynamic properties. Here, we found that the outer sphere residues, Q82 and R105, could affect the catalytic activity and product profile of Pc CHS 1. Both Q82P and R105Q mutations of Pc CHS 1 could also change the pH dependence activity as well as the product profile of Pc CHS 1. Moreover, the Q82P/C198F double mutant could rescue the complete loss of enzyme activity caused by the C198F single mutation. Our study demonstrated that these outer‐sphere residues of Pc CHS 1 play important roles both in structural maintenance and enzyme activity.