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

37 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

Bibliographical note

Publisher Copyright:
© 2016 American Chemical Society.

Access

10.1021/acs.biochem.6b01199

http://europepmc.org/articles/pmc5499249

OpenUrl availability

Full text

Cite this

@article{51e08c94390e4d89a5f1c9e8d94a3633,

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.",

year = "2017",

month = jan,

day = "17",

doi = "10.1021/acs.biochem.6b01199",

language = "English (US)",

volume = "56",

pages = "348--351",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "2",

}

TY - JOUR

T1 - β-Lactone synthetase found in the olefin biosynthesis pathway

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.

UR - http://www.scopus.com/inward/record.url?scp=85014848506&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85014848506&partnerID=8YFLogxK

U2 - 10.1021/acs.biochem.6b01199

DO - 10.1021/acs.biochem.6b01199

M3 - Article

C2 - 28029240

AN - SCOPUS:85014848506

SN - 0006-2960

VL - 56

SP - 348

EP - 351

JO - Biochemistry

JF - Biochemistry

IS - 2

ER -

β-Lactone synthetase found in the olefin biosynthesis pathway

Abstract

Bibliographical note

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this