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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-1-28
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pubmed:abstractText |
A 3.8-kb DNA fragment which was able to complement the mutation of a lysine auxotrophic Thermus thermophilus mutant was cloned from T. thermophilus HB27. Sequence analysis of the 3.8-kb fragment indicated the presence of three open reading frames including a truncated one. The predicted amino acid sequences of two of the three open reading frames showed 55.2% and 45.0% identity with homocitrate synthase and homoaconitate hydratase of Saccharomyces cerevisiae, respectively. These two enzymes act as lysine biosynthetic enzymes through the alpha-aminoadipate pathway which has been reported in S. cerevisiae and fungi. Each of the two open reading frames in T. thermophilus was disrupted by integration of the heat-stable kanamycin nucleotidyltransferase gene. The resulting mutants showed lysine auxotrophy, which could be complemented with alpha-aminoadipate but not with diaminopimelate. These results indicate that lysine was synthesized through the alpha-aminoadipate pathway and not through the diaminopimelate pathway in T. thermophilus.
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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/2-Aminoadipic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Oxo-Acid-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/homoaconitate hydratase,
http://linkedlifedata.com/resource/pubmed/chemical/homocitrate synthase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0378-1097
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
169
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
361-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9868782-2-Aminoadipic Acid,
pubmed-meshheading:9868782-Amino Acid Sequence,
pubmed-meshheading:9868782-Cloning, Molecular,
pubmed-meshheading:9868782-Genes, Bacterial,
pubmed-meshheading:9868782-Genes, Fungal,
pubmed-meshheading:9868782-Hydro-Lyases,
pubmed-meshheading:9868782-Lysine,
pubmed-meshheading:9868782-Molecular Sequence Data,
pubmed-meshheading:9868782-Mutation,
pubmed-meshheading:9868782-Open Reading Frames,
pubmed-meshheading:9868782-Oxo-Acid-Lyases,
pubmed-meshheading:9868782-Saccharomyces cerevisiae,
pubmed-meshheading:9868782-Sequence Alignment,
pubmed-meshheading:9868782-Thermus thermophilus
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pubmed:year |
1998
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pubmed:articleTitle |
Lysine is synthesized through the alpha-aminoadipate pathway in Thermus thermophilus.
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pubmed:affiliation |
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
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pubmed:publicationType |
Journal Article
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