This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Aldor, I. S.
Right arrow Articles by Keasling, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aldor, I. S.
Right arrow Articles by Keasling, J. D.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*CYANOCOBALAMIN
Agricola
Right arrow Articles by Aldor, I. S.
Right arrow Articles by Keasling, J. D.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, August 2002, p. 3848-3854, Vol. 68, No. 8
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.8.3848-3854.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Metabolic Engineering of a Novel Propionate-Independent Pathway for the Production of Poly(3-Hydroxybutyrate-co-3-Hydroxyvalerate) in Recombinant Salmonella enterica Serovar Typhimurium

Ilana S. Aldor,,{dagger} Seon-Won Kim,,{ddagger} Kristala L. Jones Prather,,§ and Jay D. Keasling*

Department of Chemical Engineering, University of California, Berkeley, California 94720-1462

Received 25 February 2002/ Accepted 14 May 2002

A pathway was metabolically engineered to produce poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV), a biodegradable thermoplastic with proven commercial applications, from a single, unrelated carbon source. An expression system was developed in which a prpC strain of Salmonella enterica serovar Typhimurium, with a mutation in the ability to metabolize propionyl coenzyme A (propionyl-CoA), served as the host for a plasmid harboring the Acinetobacter polyhydroxyalkanoate synthesis operon (phaBCA) and a second plasmid with the Escherichia coli sbm and ygfG genes under an independent promoter. The sbm and ygfG genes encode a novel (2R)-methylmalonyl-CoA mutase and a (2R)-methylmalonyl-CoA decarboxylase, respectively, which convert succinyl-CoA, derived from the tricarboxylic acid cycle, to propionyl-CoA, an essential precursor of 3-hydroxyvalerate (HV). The S. enterica system accumulated PHBV with significant HV incorporation when the organism was grown aerobically with glycerol as the sole carbon source. It was possible to vary the average HV fraction in the copolymer by adjusting the arabinose or cyanocobalamin (precursor of coenzyme B12) concentration in the medium.


* Corresponding author. Mailing address: Department of Chemical Engineering, 201 Gilman Hall, University of California, Berkeley, CA 94720-1462. Phone: (510) 642-4862. Fax: (510) 643-1228. E-mail: keasling{at}socrates.berkeley.edu.

{dagger} Present address: Genentech, Inc., South San Francisco, CA 94080.

{ddagger} Present address: Gyeongsang National University, Jinju, Korea 660-701.

§ Present address: Merck and Co., Inc., Rahway, NJ 07065.


Applied and Environmental Microbiology, August 2002, p. 3848-3854, Vol. 68, No. 8
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.8.3848-3854.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.