catabolism of gluconate in Escherichia coli

Catabolism of gluconate in Escherichia coli by Dallas Eugene Jones Download PDF EPUB FB2

On the basis of information available in the literature, gluconate dissimilation in Escherichia coli is thought to occur via the hexose monophosphate pathway.

Evidence is presented in this study that gluconate is catabolized in this organism via an inducible Entner-Doudoroff pathway. This evidence is based on chromatographic examination of end products produced from 14 C-labeled gluconate or glucose Cited by: The catabolism of gluconate in Escherichia coli Public Deposited.

Analytics × Add Author: Dallas Eugene Jones. Abstract. On the basis of information available in the literature, gluconate dissimilation in Escherichia coliis thought to occur via the hexose monophosphate pathway. Evidence is presented in this study that gluconate is catabolized in this organism via an inducible Entner-Doudoroff pathway.

This evidence is based on chromatographic examination of end products produced from 14C-labeled gluconate or glucose Cited by: Download PDF: Sorry, we are unable to provide the full text but you may find it at the following location(s): (external link). ABSTRACT.

Uptake and phosphorylation initiate the catabolism of gluconate in E. coli. Such activities conform two systems, GntI and GntII, encoded by two sets of genes differently located on the E.

coli chromosome and under different regulation. gntT. Receivedforpublication 15November Onthebasis ofinformationavailable in theliterature,gluconate dissimilation inEscherichia coli is thoughtto occur via the hexose monophosphate pathway.

Evidence is presented in this studythatgluconateis catabolized in this organism evidence is based on chromato. Summary: The utilization of gluconate as the sole source of carbon by E. coli is inducible [ Eisenberg67, Nagel73] and leads to a branch point for two central metabolic pathways: the pentose phosphate shunt and the Entner-Doudoroff pathway.

D-gluconate is imported into the cytoplasm by one of a number of gluconate transporters. A culture of a mutant of Escherichia coli, derepressed for gluconate catabolism, is killed by the addition of gluconate to the culture. The product responsible for this bactericidal effect was identified as methylglyoxal.

Two types of mutants resistant to gluconate were isolated. One of them showed increased activity of glyoxalase I. Vol number 4 FEBS LETTERS December THE FORMATION AND CATABOLISM OF METHYLGLYOXAL DURING GLYCOLYSIS IN ESCHERICHIA COLI R.A.

COOPER and Anne ANDERSON Department of Biochemistry, School of Biological Sciences, University of Leicester, Leicester, England Received 20 October 1.

Escherichia coli is still unclear (13). The discovery of a pyrroloquinoline quinone (PQQ)-dependent glucose dehy-drogenase, which catalyzes the oxidation of glucose to gluconic acid in the periplasm, suggested an alternate route for glucose catabolism in E.

coli (16). Mutants defective in enzyme I of the phosphotransferase system were able to. Mutations Affecting Gluconate Metabolism in Escherichia coli ROSANAGELDE ZWAIG, NORZWAIG,'TOMASISTORIZ,2 AND REINAS.

SANCHEZ Departamento deBiologia, Celular, Facultad de Ciencias, Universidad Central de Venezuela, ApartadoCaracas, Venezuela Received for publication 14 December   In Escherichia coli gluconate 6-phosphate is an intermediate in the oxidative catabolism of glucose, and mannonate and altronate are intermediates in the catabolism of glucuronate and galacturonate, respectively.

Although galactonate is known as an intermediate in galactose metabolism in Pseudomonads. Abstract: Following elucidation of the regulation of the lactose operon in Escherichia coli, studies on the metabolism of many sugars were initiated in the early s.

The catabolic pathways of D-gluconate and of the two hexuronates, D-glucuronate and D-galacturonate, were investigated. In E. coli, glucose metabolism mainly relies on the EMPP and the OPPP, while the EDP primarily remains inactive except during growth with gluconate [ 2 ]. The EDP utilizes only five enzymes to produce one pyruvate, one glyceraldehydephosphate, and one NADPH per glucose molecule.

Pathways of gluconate catabolism in E. coli. The first step of gluconate catabolism in E. coli is its entry into cells by gluconate permease and it is subsequently phosphorylated to gluconatephosphate by gluconate kinase. Whereas the metabolism of glucose is preferred by Escherichia coli, P. aeruginosa utilizes succinate and other tricarboxylic acid cycle intermediates before glucose (Anderson and Wood, ; Belvins et al., ; Hylemon and Phibbs, ; Midgley and Dawes, ; and Tiwari and Campbell, ).

In addition, this organism lacks an oxidative. Function i Catalyzes the reduction of 5-keto-D-gluconate to D-gluconate, using either NADH or NADPH. Is likely involved in an L-idonate degradation pathway that allows to utilize L-idonate as the sole carbon and energy source.

The classic example involves the growth of the bacterium Escherichia coli on glucose and lactose, where E. coli will consume glucose before. Regulation of enzyme (levanase) and of an extra cellular fructosyltransferase (levansucrase [Lvs]) are reviewed in this chapter. Carbohydrate catabolism in other gram-positive bacteria is in most cases less well documented than that in B.

subtilis. Catabolism of L-arabinose, D-xylose, sucrose, glycerol, and gluconate and the corresponding regulons are described in this chapter. In Escherichia coli, gluconate can be provided as an exogenous carbon source, but in addition it may be produced by the direct oxidation of glucose in the periplasm involving a membrane-bound quinoprotein glucose dehydrogenase coupled to.

Rameau dégradatif commun des hexuronates chez Escherichia coli K Mécanisme d'induction des enzymes assurant le métabolisme du 2-cétodésoxy-gluconate. Eur J Biochem. Nov 7; 30 (3)– Rekarte UD, Zwaig N, Istúriz T.

Accumulation of methylglyoxal in a mutant of Escherichia coli constitutive for gluconate catabolism.A mutant lacking gluconatephosphate dehydrase (the first enzyme of the Entner-Doudoroff pathway) was isolated after ethyl methane sulfonate mutagenesis of Escherichia coli.

Other enzymes of gluconate metabolism (gluconokinase, gluconatephosphate dehydrogenase, and 2-ketodeoxygluconatephosphate aldolase) were present in the mutant.

We constructed an Escherichia coli strain that does not use glycolysis for sugar catabolism. Instead, it uses the synthetic nonoxidative glycolysis cycle to directly synthesize stoichiometric amounts of the two-carbon building block (acetyl-CoA), which is then converted to three-carbon metabolites to support growth.

The resulting strain grows aerobically in glucose minimal .