Document Detail


A novel metabolic cycle catalyzes glucose oxidation and anaplerosis in hungry Escherichia coli.
MedLine Citation:
PMID:  12963713     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Complete oxidation of carbohydrates to CO2 is considered to be the exclusive property of the ubiquitous tricarboxylic acid cycle, the central process in cellular energy metabolism of aerobic organisms. Based on metabolism-wide in vivo quantification of intracellular carbon fluxes, we describe here complete oxidation of carbohydrates via the novel P-enolpyruvate (PEP)-glyoxylate cycle, in which two PEP molecules are oxidized by means of acetyl coenzyme A, citrate, glyoxylate, and oxaloacetate to CO2, and one PEP is regenerated. Key reactions are the constituents of the glyoxylate shunt and PEP carboxykinase, whose conjoint operation in this bi-functional catabolic and anabolic cycle is in sharp contrast to their generally recognized functions in anaplerosis and gluconeogenesis, respectively. Parallel operation of the PEP-glyoxylate cycle and the tricarboxylic acid cycle was identified in the bacterium Escherichia coli under conditions of glucose hunger in a slow-growing continuous culture. Because the PEP-glyoxylate cycle was also active in glucose excess batch cultures of an NADPH-overproducing phosphoglucose isomerase mutant, one function of this new central pathway may be the decoupling of catabolism from NADPH formation that would otherwise occur in the tricarboxylic acid cycle.
Authors:
Eliane Fischer; Uwe Sauer
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Publication Detail:
Type:  Journal Article     Date:  2003-09-08
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  278     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-11-17     Completed Date:  2004-02-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  46446-51     Citation Subset:  IM    
Affiliation:
Institute of Biotechnology, ETH Zürich, CH-8093 Zürich, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Catalysis
Citric Acid Cycle
Escherichia coli / metabolism
Escherichia coli Proteins / metabolism*
Glucose / metabolism*
Glyoxylates / metabolism
Hunger
NADP / biosynthesis
Oxidation-Reduction
Phosphoenolpyruvate / metabolism
Phosphoenolpyruvate Carboxykinase (ATP)
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Glyoxylates; 298-12-4/glyoxylic acid; 50-99-7/Glucose; 53-59-8/NADP; 73-89-2/Phosphoenolpyruvate; EC 4.1.1.49/Phosphoenolpyruvate Carboxykinase (ATP)

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


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