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Review

Terpene Biosynthesis: Modularity Rules

Prof. Dr. Dr. Eric Oldfield

Corresponding Author

E-mail address:eo@chad.scs.uiuc.edu

Department of Chemistry and Center for Biophysics and Computational Biology, University of Illinois at Urbana‐Champaign, 600 South Mathews Avenue, Urbana, IL, 61801 (USA)

Department of Chemistry and Center for Biophysics and Computational Biology, University of Illinois at Urbana‐Champaign, 600 South Mathews Avenue, Urbana, IL, 61801 (USA)
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Dr. Fu‐Yang Lin

Department of Chemistry and Center for Biophysics and Computational Biology, University of Illinois at Urbana‐Champaign, 600 South Mathews Avenue, Urbana, IL, 61801 (USA)

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First published: 21 November 2011
Cited by: 107

Abstract

Terpenes are the largest class of small‐molecule natural products on earth, and the most abundant by mass. Here, we summarize recent developments in elucidating the structure and function of the proteins involved in their biosynthesis. There are six main building blocks or modules (α, β, γ, δ, ε, and ζ) that make up the structures of these enzymes: the αα and αδ head‐to‐tail trans‐prenyl transferases that produce trans‐isoprenoid diphosphates from C5 precursors; the ε head‐to‐head prenyl transferases that convert these diphosphates into the tri‐ and tetraterpene precursors of sterols, hopanoids, and carotenoids; the βγ di‐ and triterpene synthases; the ζ head‐to‐tail cis‐prenyl transferases that produce the cis‐isoprenoid diphosphates involved in bacterial cell wall biosynthesis; and finally the α, αβ, and αβγ terpene synthases that produce plant terpenes, with many of these modular enzymes having originated from ancestral α and β domain proteins. We also review progress in determining the structure and function of the two 4Fe‐4S reductases involved in formation of the C5 diphosphates in many bacteria, where again, highly modular structures are found.

Number of times cited: 107

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