| pubmed-article:2120195 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0030844 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2120195 | lifeskim:mentions | umls-concept:C0124137 | lld:lifeskim |
| pubmed-article:2120195 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:2120195 | pubmed:dateCreated | 1990-11-14 | lld:pubmed |
| pubmed-article:2120195 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2120195 | 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. | lld:pubmed |
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| pubmed-article:2120195 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2120195 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2120195 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2120195 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2120195 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2120195 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2120195 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2120195 | pubmed:author | pubmed-author:MillerJ RJR | lld:pubmed |
| pubmed-article:2120195 | pubmed:author | pubmed-author:TobinM BMB | lld:pubmed |
| pubmed-article:2120195 | pubmed:author | pubmed-author:SkatrudP LPL | lld:pubmed |
| pubmed-article:2120195 | pubmed:author | pubmed-author:FlemingM DMD | lld:pubmed |
| pubmed-article:2120195 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2120195 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:2120195 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2120195 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2120195 | pubmed:pagination | 5908-14 | lld:pubmed |
| pubmed-article:2120195 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2120195 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2120195 | 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. | lld:pubmed |
| pubmed-article:2120195 | pubmed:affiliation | Department of Molecular Genetics Research, Lilly Research Laboratories, Indianapolis, Indiana 46285. | lld:pubmed |
| pubmed-article:2120195 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2120195 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2120195 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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