Literature DB >> 2841298

Salmonella typhimurium mutants lacking NAD pyrophosphatase.

U E Park1, J R Roth, B M Olivera.   

Abstract

NAD can serve as both a purine and a pyridine source for Salmonella typhimurium. Exogenous NAD is rapidly broken down into nicotinamide mononucleotide and AMP by an NAD pyrophosphatase, the first step in the pathway for the assimilation of exogenous NAD. We isolated and characterized mutants of S. typhimurium lacking NAD pyrophosphatase activity; such mutants were identified by their failure to use exogenous NAD as a purine source. These mutants carry mutations that map at a new locus, designated pnuE, between 86 and 87 min on the Salmonella chromosome.

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Year:  1988        PMID: 2841298      PMCID: PMC211351          DOI: 10.1128/jb.170.8.3725-3730.1988

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  18 in total

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Review 8.  Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems.

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Authors:  M P Spector; J M Hill; E A Holley; J W Foster
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10.  Pyridine nucleotide cycle of Salmonella typhimurium: in vitro demonstration of nicotinamide mononucleotide deamidase and characterization of pnuA mutants defective in nicotinamide mononucleotide transport.

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  7 in total

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2.  The stm4066 gene product of Salmonella enterica serovar Typhimurium has aminoimidazole riboside (AIRs) kinase activity and allows AIRs to satisfy the thiamine requirement of pur mutant strains.

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Authors:  G Kemmer; T J Reilly; J Schmidt-Brauns; G W Zlotnik; B A Green; M J Fiske; M Herbert; A Kraiss; S Schlör; A Smith; J Reidl
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5.  Genetic characterization of the pnuC gene, which encodes a component of the nicotinamide mononucleotide transport system in Salmonella typhimurium.

Authors:  N Zhu; B M Olivera; J R Roth
Journal:  J Bacteriol       Date:  1989-08       Impact factor: 3.490

6.  DNA ligase and the pyridine nucleotide cycle in Salmonella typhimurium.

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7.  The first comprehensive phylogenetic and biochemical analysis of NADH diphosphatases reveals that the enzyme from Tuber melanosporum is highly active towards NAD.

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  7 in total

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