Open AccessTcGLIP GDSL Lipase Substrate Specificity Co-determines the Pyrethrin Composition in Tanacetum cinerariifolium
Author(s) -
Yukimi Sugisaka,
Shiori Aoyama,
Konoka Kumagai,
Makoto Ihara,
Kazuhiko Matsuda
Publication year - 2022
Publication title -
journal of agricultural and food chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.203
H-Index - 297
eISSN - 1520-5118
pISSN - 0021-8561
DOI - 10.1021/acs.jafc.2c02365
Subject(s) - chemistry , moiety , lipase , substrate (aquarium) , substrate specificity , stereochemistry , enzyme , biochemistry , biology , ecology
Natural pesticides pyrethrins biosynthesized by Tanacetum cinrerariifolium are biodegradable and safer insecticides for pest insect control. TcGLIP, a GDSL lipase underpinning the ester bond formation in pyrethrins, exhibits high stereo-specificity for acyl-CoA and alcohol substrates. However, it is unknown how the enzyme recognizes the other structural features of the substrates and whether such specificity affects the product amount and composition in T. cinrerariifolium. We report here that the cysteamine moiety in (1 R ,3 R )-chrysanthemoyl CoA and the conjugated diene moiety in ( S )-pyrethrolone play key roles in the interactions with TcGLIP. CoA released from chrysanthemoyl CoA in the pyrethrin-forming reaction reduces the substrate affinity for TcGLIP by feedback inhibition. ( S )-Pyrethrolone shows the highest catalytic efficiency for TcGLIP, followed by ( S )-cinerolone and ( S )-jasmololone, contributing, at least in part, to determine the pyrethrin compositions in T. cinerariifolium .