exo-Brevicomin biosynthetic pathway enzymes from the Mountain Pine Beetle, Dendroctonus ponderosae

Minmin Song; Patrick Delaplain; Trang T Nguyen; Xibei Liu; Leah Wickenberg; Christopher Jeffrey; Gary J Blomquist; Claus Tittiger

doi:10.1016/j.ibmb.2014.08.002

exo-Brevicomin biosynthetic pathway enzymes from the Mountain Pine Beetle, Dendroctonus ponderosae

Insect Biochem Mol Biol. 2014 Oct:53:73-80. doi: 10.1016/j.ibmb.2014.08.002. Epub 2014 Aug 17.

Authors

Minmin Song¹, Patrick Delaplain², Trang T Nguyen³, Xibei Liu⁴, Leah Wickenberg⁵, Christopher Jeffrey⁶, Gary J Blomquist⁷, Claus Tittiger⁸

Affiliations

¹ Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA. Electronic address: min_min28@hotmail.com.
² Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA. Electronic address: delaplain@gmail.com.
³ Department of Chemistry, University of Nevada, Reno, NV 89557, USA. Electronic address: trangn@unr.edu.
⁴ Department of Chemistry, University of Nevada, Reno, NV 89557, USA. Electronic address: xibeibessie@gmail.com.
⁵ Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA. Electronic address: liyha@gmail.com.
⁶ Department of Chemistry, University of Nevada, Reno, NV 89557, USA. Electronic address: cjeffrey@unr.edu.
⁷ Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA. Electronic address: garyb@cabnr.unr.edu.
⁸ Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA. Electronic address: crt@unr.edu.

PMID: 25138711
DOI: 10.1016/j.ibmb.2014.08.002

Abstract

exoBrevicomin (exo-7-ethyl-5-methyl-6,8-dioxabicyclo[3.2.1]octane) is an important semiochemical for a number of beetle species, including the highly destructive Mountain Pine Beetle (Dendroctonus ponderosae). It is also found in other insects and the African elephant. Despite its significance, very little is known about its biosynthesis. A recent microarray analysis implicated a small cluster of three D. ponderosae genes in exo-brevicomin biosynthesis, two of which had identifiable open reading frames (Aw et al., 2010; BMC Genomics 11:215). Here we report further expression profiling of two genes in that cluster and functional analysis of their recombinantly-produced enzymes. One encodes a short-chain dehydrogenase that used NAD(P)(+) as a co-factor to catalyze the oxidation of (Z)-6-nonen-2-ol to (Z)-6-nonen-2-one. We therefore named the enzyme (Z)-6-nonen-2-ol dehydrogenase (ZnoDH). The other encodes the cytochrome P450, CYP6CR1, which epoxidized (Z)-6-nonen-2-one to 6,7-epoxynonan-2-one with very high specificity and substrate selectivity. Both the substrates and products of the two enzymes are intermediates in the exo-brevicomin biosynthetic pathway. Thus, ZnoDH and CYP6CR1 are enzymes that apparently catalyze the antepenultimate and penultimate steps in the exo-brevicomin biosynthetic pathway, respectively.

Keywords: Bark beetle; Dehydrogenase; Functional assay; Metabolic pathway; P450; Pheromone; exo-Brevicomin.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acids
Animals
Biosynthetic Pathways*
Bridged Bicyclo Compounds, Heterocyclic / metabolism*
Catalysis
Coleoptera / enzymology*
Esterases / chemistry
Female
Gene Expression Profiling
Ketones
Male
Molecular Sequence Data
Pheromones / biosynthesis*

Substances

6-nonen-2-one
Amino Acids
Bridged Bicyclo Compounds, Heterocyclic
Ketones
Pheromones
Esterases
brevicomin

Grants and funding

8 P20 GM103440-11/GM/NIGMS NIH HHS/United States