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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1991-11-4
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pubmed:databankReference |
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pubmed:abstractText |
Lysine epsilon-aminotransferase (LAT) in the beta-lactam-producing actinomycetes is considered to be the first step in the antibiotic biosynthetic pathway. Cloning of restriction fragments from Streptomyces clavuligerus, a beta-lactam producer, into Streptomyces lividans, a nonproducer that lacks LAT activity, led to the production of LAT in the host. DNA sequencing of restriction fragments containing the putative lat gene revealed a single open reading frame encoding a polypeptide with an approximately Mr 49,000. Expression of this coding sequence in Escherichia coli led to the production of LAT activity. Hence, LAT activity in S. clavuligerus is derived from a single polypeptide. A second open reading frame began immediately downstream from lat. Comparison of this partial sequence with the sequences of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D valine (ACV) synthetases from Penicillium chrysogenum and Cephalosporium acremonium and with nonribosomal peptide synthetases (gramicidin S and tyrocidine synthetases) found similarities among the open reading frames. Since mapping of the putative N and C termini of S. clavuligerus pcbAB suggests that the coding region occupies approximately 12 kbp and codes for a polypeptide related in size to the fungal ACV synthetases, the molecular characterization of the beta-lactam biosynthetic cluster between pcbC and cefE (approximately 25 kbp) is nearly complete.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1366440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1366605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-14545909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1694525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1706706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1901702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1987130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-1991735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2010361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2076552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2107074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2118102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2129535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2254285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2363718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2492500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2644235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2645274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-2654524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-3170546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-3754226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-3840476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-405455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-5045471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-6096212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-6771255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-6772093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1917855-7174523
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
173
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6223-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1917855-Amino Acid Sequence,
pubmed-meshheading:1917855-Base Sequence,
pubmed-meshheading:1917855-Escherichia coli,
pubmed-meshheading:1917855-Genes, Bacterial,
pubmed-meshheading:1917855-Genetic Linkage,
pubmed-meshheading:1917855-Genetic Vectors,
pubmed-meshheading:1917855-L-Lysine 6-Transaminase,
pubmed-meshheading:1917855-Molecular Sequence Data,
pubmed-meshheading:1917855-Oxidoreductases,
pubmed-meshheading:1917855-Peptide Synthases,
pubmed-meshheading:1917855-Streptomyces,
pubmed-meshheading:1917855-Transaminases
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pubmed:year |
1991
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pubmed:articleTitle |
Localization of the lysine epsilon-aminotransferase (lat) and delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from Streptomyces clavuligerus and production of lysine epsilon-aminotransferase activity in Escherichia coli.
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pubmed:affiliation |
Department of Molecular Genetics Research, Lilly Research Laboratories, Indianapolis, Indiana 46285.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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