Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli
Article Abstract:
Pyruvate oxidase (PoxB) has been found to contribute to Escherichia coli aerobic growth efficiency. The metabolic importance of PoxB was studied using an isogenic set of genetically engineered strains of E. coli. PoxB converts pyruvate directly to acetate and carbon dioxide. PoxB is used preferentially at low growth rates. Ability to convert pyruvate to acetylCoA by what seems to be a wasteful route via acetate benefits E coli.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
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Metabolic engineering in Escherichia coli: lowering the lipoyl domain content of the pyruvate dehydrogenase complex adversely affects the growth rate and yield
Article Abstract:
There are three lipoyl domains for each lipoate acetyltransferase (E2p) chain, in Escherichia(E.) coli pyruvate dehydrogenase complex (PDH) and all the three domains are necessary for proper growth on carbon substrates that require the PDH complex for metabolism. The AND-dependent oxidative decarboxylation of pyruvate to acetyl-CoA is catalyzed by PDH complex in E. coli. The conversion of carbon to biomass is lowered in mutants with one or two lipoyl domains per E2p. The reason for having three lipoyl domains is, however, not clear.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Enzymological and physiological consequences of restructuring the lipoyl domain content of the pyruvate dehydrogenase complex of Escherichia coli
Article Abstract:
The physiological consequences of increasing the number of lipoyl domains and the effects of inserting up to seven unlipoylatable (mutant) domains between a wild-type N-terminal domain were investigated. Plasmids with IPTG-inducible aceF-IpdA operons which express pyruvate dehydrogenase complexes were restructured and each plasmid reestablished the nutritional lesion of a strain with no PDH complex a high molecular sedimentable complex. Findings have shown that the three lipoyl domains perE2p chain is optimal and only the outer domain needs lipoylation for optimal activity.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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