β-Lactone synthetase found in the olefin biosynthesis pathway

James K. Christenson; Jack E. Richman; Matthew R. Jensen; Jennifer Y. Neufeld; Carrie M. Wilmot; Lawrence P. Wackett

doi:10.1021/acs.biochem.6b01199

β-Lactone synthetase found in the olefin biosynthesis pathway

James K. Christenson
, Jack E. Richman
, Matthew R. Jensen
, Jennifer Y. Neufeld
, Carrie M. Wilmot
, Lawrence P. Wackett

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

The first β-lactone synthetase enzyme is reported, creating an unexpected link between the biosynthesis of olefinic hydrocarbons and highly functionalized natural products. The enzyme OleC, involved in the microbial biosynthesis of long-chain olefinic hydrocarbons, reacts with syn- and anti-β-hydroxy acid substrates to yield cis- and trans-β-lactones, respectively. Protein sequence comparisons reveal that enzymes homologous to OleC are encoded in natural product gene clusters that generate β-lactone rings, suggesting a common mechanism of biosynthesis.

Original language	English (US)
Pages (from-to)	348-351
Number of pages	4
Journal	Biochemistry
Volume	56
Issue number	2
DOIs	https://doi.org/10.1021/acs.biochem.6b01199
State	Published - Jan 17 2017

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© 2016 American Chemical Society.

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http://europepmc.org/articles/pmc5499249

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title = "β-Lactone synthetase found in the olefin biosynthesis pathway",

abstract = "The first β-lactone synthetase enzyme is reported, creating an unexpected link between the biosynthesis of olefinic hydrocarbons and highly functionalized natural products. The enzyme OleC, involved in the microbial biosynthesis of long-chain olefinic hydrocarbons, reacts with syn- and anti-β-hydroxy acid substrates to yield cis- and trans-β-lactones, respectively. Protein sequence comparisons reveal that enzymes homologous to OleC are encoded in natural product gene clusters that generate β-lactone rings, suggesting a common mechanism of biosynthesis.",

author = "Christenson, \{James K.\} and Richman, \{Jack E.\} and Jensen, \{Matthew R.\} and Neufeld, \{Jennifer Y.\} and Wilmot, \{Carrie M.\} and Wackett, \{Lawrence P.\}",

note = "Publisher Copyright: {\textcopyright} 2016 American Chemical Society.",

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AU - Christenson, James K.

AU - Richman, Jack E.

AU - Jensen, Matthew R.

AU - Neufeld, Jennifer Y.

AU - Wilmot, Carrie M.

AU - Wackett, Lawrence P.

PY - 2017/1/17

Y1 - 2017/1/17

N2 - The first β-lactone synthetase enzyme is reported, creating an unexpected link between the biosynthesis of olefinic hydrocarbons and highly functionalized natural products. The enzyme OleC, involved in the microbial biosynthesis of long-chain olefinic hydrocarbons, reacts with syn- and anti-β-hydroxy acid substrates to yield cis- and trans-β-lactones, respectively. Protein sequence comparisons reveal that enzymes homologous to OleC are encoded in natural product gene clusters that generate β-lactone rings, suggesting a common mechanism of biosynthesis.

AB - The first β-lactone synthetase enzyme is reported, creating an unexpected link between the biosynthesis of olefinic hydrocarbons and highly functionalized natural products. The enzyme OleC, involved in the microbial biosynthesis of long-chain olefinic hydrocarbons, reacts with syn- and anti-β-hydroxy acid substrates to yield cis- and trans-β-lactones, respectively. Protein sequence comparisons reveal that enzymes homologous to OleC are encoded in natural product gene clusters that generate β-lactone rings, suggesting a common mechanism of biosynthesis.

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JO - Biochemistry

JF - Biochemistry

IS - 2

ER -

β-Lactone synthetase found in the olefin biosynthesis pathway

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