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Methods Enzymol. 2016;576:147-65. doi: 10.1016/bs.mie.2016.03.013. Epub 2016 Mar 28.

Generation and Functional Evaluation of Designer Monoterpene Synthases.

Author information

1
Institute of Biological Chemistry, M. J. Murdock Metabolomics Laboratory, Washington State University, Pullman, WA, United States.
2
Institute of Biological Chemistry, M. J. Murdock Metabolomics Laboratory, Washington State University, Pullman, WA, United States. Electronic address: lange-m@wsu.edu.

Abstract

Monoterpene synthases are highly versatile enzymes that catalyze the first committed step in the pathways toward terpenoids, the structurally most diverse class of plant natural products. Recent advancements in our understanding of the reaction mechanism have enabled engineering approaches to develop mutant monoterpene synthases that produce specific monoterpenes. In this chapter, we are describing protocols to introduce targeted mutations, express mutant enzyme catalysts in heterologous hosts, and assess their catalytic properties. Mutant monoterpene synthases have the potential to contribute significantly to synthetic biology efforts aimed at producing larger amounts of commercially attractive monoterpenes.

KEYWORDS:

Isoprenoid; Mechanism; Mutagenesis; Protein engineering; Terpene synthase; Terpenoid

PMID:
27480686
DOI:
10.1016/bs.mie.2016.03.013
[Indexed for MEDLINE]

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