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Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther.


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.

SUBMITTER: Yao JY 

PROVIDER: S-EPMC6696123 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Characterization of a <i>Cis</i>-Prenyltransferase from <i>Lilium longiflorum</i> Anther.

Yao Jyun-Yu JY   Teng Kuo-Hsun KH   Liu Ming-Che MC   Wang Co-Shine CS   Liang Po-Huang PH  

Molecules (Basel, Switzerland) 20190726 15


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). <i>cis</i>-Prenyltransferases, which catalyze <i>cis</i>-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 <i>cis</i>-prenyltr  ...[more]

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