Document Detail

Metabolic pathway structures for recombinant protein synthesis in Escherichia coli.
MedLine Citation:
PMID:  15739064     Owner:  NLM     Status:  MEDLINE    
Escherichia coli is a valuable commercial host for the production of heterologous proteins. We used elementary mode analysis to identify all possible genetically independent pathways for the production of three specific recombinant proteins, green fluorescent protein, savinase and an artificial protein consisting of repeating units of a five-amino-acid cassette. Analysis of these pathways led to the identification of the most efficient pathways for the production of each of these proteins. The results indicate that the amino acid composition of expressed proteins has a profound effect on the number and identity of possible pathways for the production of these proteins. We show that several groups of elementary modes produce the same ratio of biomass and recombinant protein. The pattern of occurrence of these modes is dependent on the amino acid composition of the specific foreign protein produced. These pathways are formed as systemic combinations of other pathways that produce biomass or foreign protein alone after the elimination of fluxes in specific internal reversible reactions or the reversible carbon dioxide exchange reaction. Since these modes represent pathway options that enable the cell to produce biomass and protein without utilizing these reactions, removal of these reactions would constrain the cells to utilize these modes for producing biomass and foreign protein at constant ratios.
Natarajan Vijayasankaran; Ross Carlson; Friedrich Srienc
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2005-10-13
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  68     ISSN:  0175-7598     ISO Abbreviation:  Appl. Microbiol. Biotechnol.     Publication Date:  2005 Oct 
Date Detail:
Created Date:  2005-10-26     Completed Date:  2005-12-01     Revised Date:  2012-07-10    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  737-46     Citation Subset:  IM    
Department of Chemical Engineering and Materials Science, University of Minnesota, 151 Amundson Hall, 421 Washington Avenue S.E., Minneapolis, MN 55455-0321, USA.
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MeSH Terms
Biotechnology / methods
Escherichia coli / genetics,  metabolism*
Green Fluorescent Proteins / chemistry,  genetics,  metabolism*
Peptides / chemistry,  genetics,  metabolism*
Protein Engineering / methods
Recombinant Proteins / chemistry,  genetics,  metabolism*
Serine Endopeptidases / chemistry,  genetics,  metabolism*
Reg. No./Substance:
0/Peptides; 0/Recombinant Proteins; 147336-22-9/Green Fluorescent Proteins; EC 3.4.21.-/Serine Endopeptidases; EC serine proteinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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