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Article

Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coli.

Journal of bioscience and bioengineering - 1 Mar 2012

Mueller Alexander P, Nomura Christopher T

Abstract excerpt

Polyhydroxyalkanoate (PHA) production has been enhanced with engineered 3-ketoacyl-ACP synthase III (FabH) enzymes that accept diverse fatty acyl-ACP substrates and convert them to fatty acyl-CoA substrates for polymerization by PHA synthase enzymes resulting in the production of diverse polymers. Two mutations in the monomer supplying enzyme FabH, His244Ala and the Asn274Ala, were investigated to assess the...

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PMID: 22143070
DOI: 10.1016/j.jbiosc.2011.10.022

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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