Elsevier

Methods in Enzymology

Volume 515, 2012, Pages 123-162
Methods in Enzymology

Chapter Seven - Diversity and Analysis of Bacterial Terpene Synthases

https://doi.org/10.1016/B978-0-12-394290-6.00007-0Get rights and content

Abstract

Terpenoid compounds are generally considered to be plant or fungal metabolites, although a small number of odorous terpenoid metabolites of bacterial origin have been known for many years. Recently, extensive bacterial genome sequencing and bioinformatic analysis of deduced bacterial proteins using a profile hidden Markov model have revealed more than a hundred distinct predicted terpene synthase genes. Although some of these synthase genes might be silent in the parent microorganisms under normal laboratory culture conditions, the controlled overexpression of these genes in a versatile heterologous host has made it possible to identify the biochemical function of cryptic genes and isolate new terpenoid metabolites.

Section snippets

Terpenoid Metabolites from Bacterial Cultures

Tens of thousands of terpenoid metabolites, including monoterpenes, sesquiterpenes, and diterpenes, are present in both terrestrial and marine higher plants, in liverworts, and in fungi, with only a relatively minor fraction having been isolated from prokaryotes. These compounds act as antibiotics, hormones, flavor or odor constituents, and pigments. Some of them also possess other physiologically or commercially important properties, such as vitamins (A, D, E, K, and coenzyme Q) and antitumor

Bacterial Terpene Synthases

Several cyclic monoterpene, sesquiterpene, and diterpene hydrocarbons and alcohols are formed by variations of the common terpene cyclization mechanism that is initiated by enzyme-catalyzed ionization to form allylic cations from the universal acyclic precursors, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), and geranylgeranyl diphosphate (GGPP) that are themselves synthesized by mechanistically related condensations of the 5-carbon building blocks dimethylallyl diphosphate (DMAPP) and

Properties of terpene synthases and database search procedures

Monoterpene, sesquiterpene, and diterpene synthases from plants and fungi have a strongly conserved amino acid sequence homology. Conversely, bacterial terpene synthases not only exhibit no significant overall sequence amino acid similarity to those from plants and fungi but also usually exhibit relatively low mutual sequence similarity to each other. Despite the very substantial differences in overall primary amino acid sequence, terpene synthases from plants, fungi, and bacteria typically

References (59)

  • D.E. Cane et al.

    Geosmin biosynthesis in Streptomyces avermitilis. Molecular cloning, expression, and mechanistic study of the germacradienol/geosmin synthase

    The Journal of Antibiotics

    (2006)
  • D.E. Cane et al.

    The biosynthesis of pentalenene and pentalenolactone

    Journal of the American Chemical Society

    (1990)
  • D.E. Cane et al.

    Pentalenene synthase. Purification, molecular cloning, sequencing and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319

    Biochemistry

    (1994)
  • D.E. Cane et al.

    Epicubenol synthase and the enzymic cyclization of farnesyl diphosphate

    Journal of the American Chemical Society

    (1993)
  • D.E. Cane et al.

    Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis

    Proceedings of the National Academy of Sciences of the United States of America

    (2003)
  • W.K. Chou et al.

    Genome mining in Streptomyces avermitilis: Cloning and characterization of SAV_76, the synthase for a new sesquiterpene, avermitilol

    Journal of the American Chemical Society

    (2010)
  • D.W. Christianson

    Structural biology and chemistry of the terpenoid cyclases

    Chemical Reviews

    (2006)
  • T. Dairi et al.

    Eubacterial diterpene cyclase genes essential for production of the isoprenoid antibiotic terpentecin

    Journal of Bacteriology

    (2001)
  • B. Felicetti et al.

    Aristolochene synthase: Mechanistic analysis of active site residues by site-directed mutagenesis

    Journal of the American Chemical Society

    (2004)
  • R.D. Finn et al.

    The Pfam protein families database

    Nucleic Acids Research

    (2010)
  • N.N. Gerber

    Geosmin, an earthy-smelling substance isolated from actinomycetes

    Biotechnology and Bioengineering

    (1967)
  • N.N. Gerber

    A volatile metabolite of actinomycetes, 2-methylisoborneol

    The Journal of Antibiotics

    (1969)
  • N.N. Gerber et al.

    Geosmin, an earthy-smelling substance isolated from actinomycetes

    Applied Microbiology

    (1965)
  • S. Giglio et al.

    Biosynthesis of 2-methylisoborneol in cyanobacteria

    Environmental Science and Technology

    (2011)
  • S. Giglio et al.

    Isolation and characterization of the gene associated with geosmin production in cyanobacteria

    Environmental Science and Technology

    (2008)
  • J.S. Glasby

    Encyclopedia of the terpenoids

    (1982)
  • B. Gust et al.

    PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin

    Proceedings of the National Academy of Sciences of the United States of America

    (2003)
  • H. Harada et al.

    Efficient synthesis of functional isoprenoids from acetoacetate through metabolic pathway-engineered Escherichia coli

    Applied Microbiology and Biotechnology

    (2009)
  • H. Ikeda et al.

    Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis

    Nature Biotechnology

    (2003)
  • Cited by (0)

    View full text