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

Paper ID Volume ID Publish Year Pages File Format Full-Text
21261 43214 2012 7 PDF Available
Title
Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coli
Abstract

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 impact of these mutations on PHA monomer production. PHA production increased more than six-fold with the mutation His244Ala in the FabH enzyme. Engineering of the FabH enzyme for improved PHA monomer supply led to a more productive system for PHA copolymer production.

Keywords
Recombinant Escherichia coli; Protein engineering; polyhydroxyalkanoates; Bioplastic; 3-Ketoacyl-ACP synthase III; fabH
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Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coli
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 113, Issue 3, March 2012, Pages 300–306
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us