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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1990-11-14
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pubmed:databankReference |
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pubmed:abstractText |
The final step in the biosynthesis of beta-lactam antibiotics in Penicillium chrysogenum and Aspergillus nidulans involves removal of the L-alpha-aminoadipyl side chain from isopenicillin N (IPN) and exchange with a nonpolar side chain. The enzyme catalyzing this reaction, acyl-coenzyme A:isopenicillin N acyltransferase (acyltransferase), was purified from P. chrysogenum and A. nidulans. Based on NH2-terminal amino acid sequence information, the acyltransferase gene (penDE) from P. chrysogenum and A. nidulans were cloned. In both organisms, penDE was located immediately downstream from the isopenicillin N synthetase gene (pcbC) and consisted of four exons encoding an enzyme of 357 amino acids (approximately 40 kilodaltons [kDa]). The DNA coding sequences showed approximately 73% identity, while the amino acid sequences were approximately 76% identical. Noncoding DNA regions (including the region between pcbC and penDE) were not conserved. Acyltransferase activity from Escherichia coli producing the 40-kDa protein accepted either 6-aminopenicillanic acid or IPN as the substrate and made a penicillinase-sensitive antibiotic in the presence of phenylacetyl coenzyme A. Therefore, a single gene is responsible for converting IPN to penicillin G. The active form of the enzyme may result from processing of the 40-kDa monomeric precursor to a heterodimer containing subunits of 11 and 29 kDa.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2107074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2110531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2166227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-237211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2511425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2555269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2644235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2654524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2829713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-2985470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3025146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3045077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3104145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3170343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3333340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3534891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-3818447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-518835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-5727632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2120195-6546423
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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 |
172
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5908-14
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2120195-Acyltransferases,
pubmed-meshheading:2120195-Amino Acid Sequence,
pubmed-meshheading:2120195-Aspergillus nidulans,
pubmed-meshheading:2120195-Base Sequence,
pubmed-meshheading:2120195-Cloning, Molecular,
pubmed-meshheading:2120195-Escherichia coli,
pubmed-meshheading:2120195-Genes, Fungal,
pubmed-meshheading:2120195-Genetic Vectors,
pubmed-meshheading:2120195-Molecular Sequence Data,
pubmed-meshheading:2120195-Penicillin-Binding Proteins,
pubmed-meshheading:2120195-Penicillium chrysogenum,
pubmed-meshheading:2120195-Plasmids,
pubmed-meshheading:2120195-Recombinant Proteins,
pubmed-meshheading:2120195-Restriction Mapping,
pubmed-meshheading:2120195-Sequence Homology, Nucleic Acid
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pubmed:year |
1990
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pubmed:articleTitle |
Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme 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,
Comparative Study,
Research Support, Non-U.S. Gov't
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