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Article

Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.

The Journal of biological chemistry - 23 Dec 2016

Goblirsch Brandon R, Jensen Matthew R, Mohamed Fatuma A, Wackett Lawrence P, Wilmot Carrie M

Abstract excerpt

Phylogenetically diverse microbes that produce long chain, olefinic hydrocarbons have received much attention as possible sources of renewable energy biocatalysts. One enzyme that is critical for this process is OleA, a thiolase superfamily enzyme that condenses two fatty acyl-CoA substrates to produce a β-ketoacid product and initiates the biosynthesis of long chain olefins in bacteria. Thiolases typically...

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Identifiers

PMID: 27815501
DOI: 10.1074/jbc.M116.760892
PMCID: PMC5207179

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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