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Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther

Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther

Jyun-Yu Yao, Kuo-Hsun Teng, Ming-Che Liu, Co-Shine Wang, Po-Huang Liang

Molecules. 2019 Jul 26;24(15):2728.

PMID: 31357567

Abstract:

A group of prenyltransferases catalyze chain elongation of farnesyl diphosphate (FPP) to designated lengths via consecutive condensation reactions with specific numbers of isopentenyl diphosphate (IPP). cis-Prenyltransferases, which catalyze cis-double bond formation during IPP condensation, usually synthesize long-chain products as lipid carriers to mediate peptidoglycan biosynthesis in prokaryotes and protein glycosylation in eukaryotes. Unlike only one or two cis-prenyltransferases in bacteria, yeast, and animals, plants have several cis-prenyltransferases and their functions are less understood. As reported here, a cis-prenyltransferase from Lilium longiflorum anther, named LLA66, was expressed in Saccharomyces cerevisiae and characterized to produce C40/C45 products without the capability to restore the growth defect from Rer2-deletion, although it was phylogenetically categorized as a long-chain enzyme. Our studies suggest that evolutional mutations may occur in the plant cis-prenyltransferase to convert it into a shorter-chain enzyme.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
LS741322	Peptidoglycan from Saccharomyces cerevisiae			Price

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