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Open AccessArticle

Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther

Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan
Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan
Graduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, Taiwan
Author to whom correspondence should be addressed.
Academic Editors: Ewa Swiezewska, Liliana Surmacz and Bernhard Loll
Molecules 2019, 24(15), 2728;
Received: 27 June 2019 / Revised: 19 July 2019 / Accepted: 25 July 2019 / Published: 26 July 2019
(This article belongs to the Special Issue Plant Isoprenoids)
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. View Full-Text
Keywords: isoprenoid; prenyltransferase; polyisoprenoid; dolichol; glycoprotein isoprenoid; prenyltransferase; polyisoprenoid; dolichol; glycoprotein
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Yao, J.-Y.; Teng, K.-H.; Liu, M.-C.; Wang, C.-S.; Liang, P.-H. Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther. Molecules 2019, 24, 2728.

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