PMID:16153292: Difference between revisions

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<span style = 'font-size: large'> '''Stancek, M, Schnell, R and Rydén-Aulin, M'''  (2005) Analysis of Escherichia coli nicotinate mononucleotide adenylyltransferase mutants in vivo and in vitro.''BMC Biochem.'' '''6''':16</span>
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|{{TableHeadingColor}} |'''Abstract''' || BACKGROUND: Adenylation of nicotinate mononucleotide to nicotinate adenine dinucleotide is the penultimate step in NAD+ synthesis. In Escherichia coli, the enzyme nicotinate mononucleotide adenylyltransferase is encoded by the nadD gene. We have earlier made an initial characterization in vivo of two mutant enzymes, NadD72 and NadD74. Strains with either mutation have decreased intracellular levels of NAD+, especially for one of the alleles, nadD72. RESULTS: In this study these two mutant proteins have been further characterized together with ten new mutant variants. Of the, in total, twelve mutations four are in a conserved motif in the C-terminus and eight are in the active site. We have tested the activity of the enzymes in vitro and their effect on the growth phenotype in vivo. There is a very good correlation between the two data sets. CONCLUSION: The mutations in the C-terminus did not reveal any function for the conserved motif. On the other hand, our data has lead us to assign amino acid residues His-19, Arg-46 and Asp-109 to the active site. We have also shown that the nadD gene is essential for growth in E. coli.
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'''Stancek, M, Schnell, R and Rydén-Aulin, M'''  (2005) Analysis of Escherichia coli nicotinate mononucleotide adenylyltransferase mutants in vivo and in vitro. ''BMC Biochem.'' '''6''':16
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Adenylation of nicotinate mononucleotide to nicotinate adenine dinucleotide is the penultimate step in NAD+ synthesis. In Escherichia coli, the enzyme nicotinate mononucleotide adenylyltransferase is encoded by the nadD gene. We have earlier made an initial characterization in vivo of two mutant enzymes, NadD72 and NadD74. Strains with either mutation have decreased intracellular levels of NAD+, especially for one of the alleles, nadD72.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16153292 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1249556 PMC1249556]
Online version:[http://dx.doi.org/10.1186/1471-2091-6-16 10.1186/1471-2091-6-16]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16153292 PubMed]
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Binding Sites/physiology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutation; Nicotinamide-Nucleotide Adenylyltransferase/chemistry; Nicotinamide-Nucleotide Adenylyltransferase/genetics; Nicotinamide-Nucleotide Adenylyltransferase/metabolism; Protein Conformation
 
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Latest revision as of 04:28, 15 September 2013

Citation

Stancek, M, Schnell, R and Rydén-Aulin, M (2005) Analysis of Escherichia coli nicotinate mononucleotide adenylyltransferase mutants in vivo and in vitro. BMC Biochem. 6:16

Abstract

Adenylation of nicotinate mononucleotide to nicotinate adenine dinucleotide is the penultimate step in NAD+ synthesis. In Escherichia coli, the enzyme nicotinate mononucleotide adenylyltransferase is encoded by the nadD gene. We have earlier made an initial characterization in vivo of two mutant enzymes, NadD72 and NadD74. Strains with either mutation have decreased intracellular levels of NAD+, especially for one of the alleles, nadD72.

Links

PubMed PMC1249556 Online version:10.1186/1471-2091-6-16

Keywords

Binding Sites/physiology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutation; Nicotinamide-Nucleotide Adenylyltransferase/chemistry; Nicotinamide-Nucleotide Adenylyltransferase/genetics; Nicotinamide-Nucleotide Adenylyltransferase/metabolism; Protein Conformation

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