| pubmed-article:8344300 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0030844 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0001390 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0002488 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C1149781 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:8344300 | lifeskim:mentions | umls-concept:C0051653 | lld:lifeskim |
| pubmed-article:8344300 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8344300 | pubmed:dateCreated | 1993-9-3 | lld:pubmed |
| pubmed-article:8344300 | pubmed:abstractText | The isopenicillin-N acyltransferase of Penicillium chrysogenum catalyzes the conversion of the biosynthetic intermediate isopenicillin N to the hydrophobic penicillins. The isopenicillin-N acyltransferase copurified with the acyl-CoA:6-aminopenicillanic acid (6-APA) acyltransferase activity which transfers an acyl residue from acyl-CoA derivatives (e.g. phenylacetyl-CoA, phenoxyacetyl-CoA) to 6-APA. Other thioesters of phenylacetic acid were also used as substrates. An amino acid sequence similar to that of the active site of thioesterases was found in the isopenicillin-N acyltransferase, suggesting that this site is involved in the transfer of phenylacetyl residues from phenylacetyl thioesters. Purified isopenicillin-N acyltransferase also showed isopenicillin-N amidohydrolase, penicillin transacylase and penicillin amidase activities. The isopenicillin-N amidohydrolase (releasing 6-APA) showed a much lower specific activity than the isopenicillin-N acyltransferase of the same enzyme preparation, suggesting that in the isopenicillin-N acyltransferase reaction the 6-APA is not released and is directly converted into benzylpenicillin. Penicillin transacylase exchanged side chains between two hydrophobic penicillin molecules; or between one penicillin molecule and 6-APA. The penicillin amidase activity is probably the reverse of the biosynthetic acyl-CoA:6-APA acyltransferase. Four P. chrysogenum mutants deficient in acyl-CoA:6-APA acyltransferase lacked the other four related activities. Transformation of these mutants with the penDE gene restored all five enzyme activities. | lld:pubmed |
| pubmed-article:8344300 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8344300 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8344300 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8344300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8344300 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8344300 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8344300 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:MartínJ FJF | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:MeesschaertBB | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:AlvarezEE | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:GutiérrezSS | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:JuryE IEI | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:MontenegroEE | lld:pubmed |
| pubmed-article:8344300 | pubmed:author | pubmed-author:BarredoJ LJL | lld:pubmed |
| pubmed-article:8344300 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8344300 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8344300 | pubmed:volume | 215 | lld:pubmed |
| pubmed-article:8344300 | pubmed:geneSymbol | penDE | lld:pubmed |
| pubmed-article:8344300 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8344300 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8344300 | pubmed:pagination | 323-32 | lld:pubmed |
| pubmed-article:8344300 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:8344300 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8344300 | pubmed:articleTitle | The isopenicillin-N acyltransferase of Penicillium chrysogenum has isopenicillin-N amidohydrolase, 6-aminopenicillanic acid acyltransferase and penicillin amidase activities, all of which are encoded by the single penDE gene. | lld:pubmed |
| pubmed-article:8344300 | pubmed:affiliation | Department of Ecology, Genetics and Microbiology, Faculty of Biology, University of Leon, Spain. | lld:pubmed |
| pubmed-article:8344300 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8344300 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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