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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-9-20
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pubmed:abstractText |
The two genes, nadA and nadB, responsible for quinolinate biosynthesis from aspartate and dihydroxyacetone phosphate in Escherichia coli were cloned and characterized. Quinolinate (pyridine-2,3-dicarboxylate) is the biosynthetic precursor of the pyridine ring of NAD. Gene nadA was identified by complementation in three different nadA mutant strains. Sequence analysis provided an 840-bp open reading frame coding for a 31,555-Da protein. Gene nadB was identified by complementation in a nadB mutant strain and by the L-aspartate oxidase activity of its gene product. Sequence analysis showed a 1620-bp open reading frame coding for a 60,306-Da protein. For both genes, promoter regions and ribosomal binding sites were assigned by comparison to consensus sequences. The nadB gene product, L-aspartate oxidase, was purified to homogeneity and the N-terminal sequence of 19 amino acids was determined. The enzyme was shown to be specific for L-aspartate. High-copy-number vectors, carrying either gene nadA, nadB or nadA + nadB, increased quinolinate production 1.5-fold, 2.0-fold and 15-fold respectively. Both gene products seem to be equally rate-limiting in quinolinate synthesis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Restriction Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/L-aspartate oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolinic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolinic Acids
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
175
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
221-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2841129-Amino Acid Oxidoreductases,
pubmed-meshheading:2841129-Amino Acid Sequence,
pubmed-meshheading:2841129-Bacterial Proteins,
pubmed-meshheading:2841129-Base Sequence,
pubmed-meshheading:2841129-Cloning, Molecular,
pubmed-meshheading:2841129-DNA Restriction Enzymes,
pubmed-meshheading:2841129-Escherichia coli,
pubmed-meshheading:2841129-Genes,
pubmed-meshheading:2841129-Genes, Bacterial,
pubmed-meshheading:2841129-Molecular Sequence Data,
pubmed-meshheading:2841129-NAD,
pubmed-meshheading:2841129-Plasmids,
pubmed-meshheading:2841129-Promoter Regions, Genetic,
pubmed-meshheading:2841129-Pyridines,
pubmed-meshheading:2841129-Quinolinic Acid,
pubmed-meshheading:2841129-Quinolinic Acids
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pubmed:year |
1988
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pubmed:articleTitle |
Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB.
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pubmed:affiliation |
Institut für Biochemie, Technische Hochschule Darmstadt, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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