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Updated: Mar 7, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Expanding the product portfolio of fungal type I fatty acid synthases
Zhiwei Zhu1,2,3, Yongjin J Zhou1,3, Anastasia Krivoruchko1,3,4
1Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden.
Abstract:
Fungal type I fatty acid synthases (FASs) are mega-enzymes with two separated, identical compartments, in which the acyl carrier protein (ACP) domains shuttle substrates to catalytically active sites embedded in the chamber wall. We devised synthetic FASs by integrating heterologous enzymes into the reaction chambers and demonstrated their capability to convert acyl-ACP or acyl-CoA from canonical fatty acid biosynthesis to short/medium-chain fatty acids and methyl ketones.
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