Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass

Chemical Science
Masahiro FujihashiKunio Miki

Abstract

Thousands of terpenes have been identified to date. However, only two classes of enzymes are known to be involved in their biosynthesis, and each class has characteristic amino-acid motifs. We recently identified a novel large-terpene (C25/C30/C35) synthase, which shares no motifs with known enzymes. To elucidate the molecular mechanism of this enzyme, we determined the crystal structure of a large-β-prene synthase from B. alcalophilus (BalTS). Surprisingly, the overall structure of BalTS is similar to that of the α-domain of class I terpene synthases although their primary structures are totally different from each other. Two novel aspartate-rich motifs, DYLDNLxD and DY(F,L,W)IDxxED, are identified, and mutations of any one of the aspartates eliminate its enzymatic activity. The present work leads us to propose a new subclass of terpene synthases, class IB, which is probably responsible for large-terpene biosynthesis.

References

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May 12, 2010·Nucleic Acids Research·Liisa Holm, Päivi Rosenström
Nov 23, 2011·Angewandte Chemie·Eric Oldfield, Fu-Yang Lin
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Citations

Jun 22, 2018·Angewandte Chemie·Daijiro UedaTsutomu Sato
Oct 28, 2019·Natural Product Reports·Jeffrey D Rudolf, Chin-Yuan Chang
May 28, 2020·Proceedings of the National Academy of Sciences of the United States of America·Jonathan R ChekanBradley S Moore
Nov 28, 2020·IUBMB Life·Hsin-Yang ChangAndrew H-J Wang
Jul 15, 2021·Proceedings of the National Academy of Sciences of the United States of America·Rong ChenTiangang Liu

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Software Mentioned

DALI
BalTS
BclTS
BLAST

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