Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli

Corynebacterium glutamicum is widely used in the industrial production of amino acids. We have found that this bacterium grows exponentially on a mineral médium supplemented with gluconate. Gluconate permease and Gluconokinase are expressed in an inducible form and, 6-phosphogluconate dehydrogenase,...

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Autores principales: PORCO,ANTONIETTA, GAMERO,ELIDA E, MYLONÁS,ELENA, ISTÚRIZ,TOMÁS
Lenguaje:English
Publicado: Sociedad de Biología de Chile 2008
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gnt
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300011
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spelling oai:scielo:S0716-976020080003000112009-04-23Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coliPORCO,ANTONIETTAGAMERO,ELIDA EMYLONÁS,ELENAISTÚRIZ,TOMÁS Corynebacterium glutamicum gluconate metabolism gnt Corynebacterium glutamicum is widely used in the industrial production of amino acids. We have found that this bacterium grows exponentially on a mineral médium supplemented with gluconate. Gluconate permease and Gluconokinase are expressed in an inducible form and, 6-phosphogluconate dehydrogenase, although constituvely expressed, shows a 3-fold higher specific level in gluconate grown cells than those grown in fructose under similar conditions. Interestingly, these activities are lower than those detected in the strain Escherichia coli Ml-8, cultivated under similar conditions. Additionally, here we also confirmed that this bacterium lacks 6-phosphogluconate dehydratase activity. Thus, gluconate must be metabolized through the pentose phosphate pathway. Genes encoding gluconate transport and its phosphorylation were cloned from C. glutamicum, and expressed in suitable E. coli mutants. Sequence analysis revealed that the amino acid sequences obtained from these genes, denoted as gntP and gntK, were similar to those found in other bacteria. Analysis of both genes by RT-PCR suggested constitutive expression, in disagreement with the inducible character of their corresponding activities. The results suggest that gluconate might be a suitable source of reduction potential for improving the efficiency in cultures engaged in amino acids production. This is the first time that gluconate specific enzymatic activities are reported in C. glutamicum.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.41 n.3 20082008-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300011en10.4067/S0716-97602008000300011
institution Scielo Chile
collection Scielo Chile
language English
topic Corynebacterium glutamicum
gluconate metabolism
gnt
spellingShingle Corynebacterium glutamicum
gluconate metabolism
gnt
PORCO,ANTONIETTA
GAMERO,ELIDA E
MYLONÁS,ELENA
ISTÚRIZ,TOMÁS
Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
description Corynebacterium glutamicum is widely used in the industrial production of amino acids. We have found that this bacterium grows exponentially on a mineral médium supplemented with gluconate. Gluconate permease and Gluconokinase are expressed in an inducible form and, 6-phosphogluconate dehydrogenase, although constituvely expressed, shows a 3-fold higher specific level in gluconate grown cells than those grown in fructose under similar conditions. Interestingly, these activities are lower than those detected in the strain Escherichia coli Ml-8, cultivated under similar conditions. Additionally, here we also confirmed that this bacterium lacks 6-phosphogluconate dehydratase activity. Thus, gluconate must be metabolized through the pentose phosphate pathway. Genes encoding gluconate transport and its phosphorylation were cloned from C. glutamicum, and expressed in suitable E. coli mutants. Sequence analysis revealed that the amino acid sequences obtained from these genes, denoted as gntP and gntK, were similar to those found in other bacteria. Analysis of both genes by RT-PCR suggested constitutive expression, in disagreement with the inducible character of their corresponding activities. The results suggest that gluconate might be a suitable source of reduction potential for improving the efficiency in cultures engaged in amino acids production. This is the first time that gluconate specific enzymatic activities are reported in C. glutamicum.
author PORCO,ANTONIETTA
GAMERO,ELIDA E
MYLONÁS,ELENA
ISTÚRIZ,TOMÁS
author_facet PORCO,ANTONIETTA
GAMERO,ELIDA E
MYLONÁS,ELENA
ISTÚRIZ,TOMÁS
author_sort PORCO,ANTONIETTA
title Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
title_short Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
title_full Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
title_fullStr Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
title_full_unstemmed Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: Cloning and expression of gntP and gntK in Escherichia coli
title_sort gluconate as suitable potential reduction supplier in corynebacterium glutamicum: cloning and expression of gntp and gntk in escherichia coli
publisher Sociedad de Biología de Chile
publishDate 2008
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300011
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