{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T10:26:24Z","timestamp":1785234384232,"version":"3.55.0"},"reference-count":47,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,4,1]]},"abstract":"<jats:p>A gene, phl, encoding a phenylacetyl-CoA ligase was cloned from a phage library of Penicillium chrysogenum AS-P-78. The presence of five introns in the phl gene was confirmed by reverse transcriptase-PCR. The phl gene encoded an aryl-CoA ligase closely related to Arabidopsis thaliana 4-coumaroyl-CoA ligase. The Phl protein contained most of the amino acids defining the aryl-CoA (4-coumaroyl-CoA) ligase substrate-specificity code and differed from acetyl-CoA ligase and other acyl-CoA ligases. The phl gene was not linked to the penicillin gene cluster. Amplification of phl in an autonomous replicating plasmid led to an 8-fold increase in phenylacetyl-CoA ligase activity and a 35% increase in penicillin production. Transformants containing the amplified phl gene were resistant to high concentrations of phenylacetic acid (more than 2.5\u00a0g\/l). Disruption of the phl gene resulted in a 40% decrease in penicillin production and a similar reduction of phenylacetyl-CoA ligase activity. The disrupted mutants were highly susceptible to phenylacetic acid. Complementation of the disrupted mutants with the phl gene restored normal levels of penicillin production and resistance to phenylacetic acid. The phenylacetyl-CoA ligase encoded by the phl gene is therefore involved in penicillin production, although a second aryl-CoA ligase appears to contribute partially to phenylacetic acid activation. The Phl protein lacks a peptide-carrier-protein domain and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase. The Phl protein contains the peroxisome-targeting sequence that is also present in the isopenicillin N acyltransferase. The peroxisomal co-localization of these two proteins indicates that the last two enzymes of the penicillin pathway form a peroxisomal functional complex.<\/jats:p>","DOI":"10.1042\/bj20051599","type":"journal-article","created":{"date-parts":[[2006,3,15]],"date-time":"2006-03-15T16:56:53Z","timestamp":1142441813000},"page":"147-155","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":77,"title":["Amplification and disruption of the phenylacetyl-CoA ligase gene of <i>Penicillium chrysogenum<\/i> encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N-acyltransferase"],"prefix":"10.1042","volume":"395","author":[{"given":"M\u00f3nica","family":"Lamas-Maceiras","sequence":"first","affiliation":[{"name":"\u00c1rea de Microbiolog\u00eda, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, Campus de Vegazana, s\/n, 24071 Le\u00f3n, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inmaculada","family":"Vaca","sequence":"additional","affiliation":[{"name":"Instituto de Biotecnolog\u00eda de Le\u00f3n, INBIOTEC, Parque Cient\u00edfico de Le\u00f3n, 1 Av. Real, 24006 Le\u00f3n, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Esther","family":"Rodr\u00edguez","sequence":"additional","affiliation":[{"name":"\u00c1rea de Microbiolog\u00eda, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, Campus de Vegazana, s\/n, 24071 Le\u00f3n, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Javier","family":"Casqueiro","sequence":"additional","affiliation":[{"name":"\u00c1rea de Microbiolog\u00eda, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, Campus de Vegazana, s\/n, 24071 Le\u00f3n, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan\u00a0F.","family":"Mart\u00edn","sequence":"additional","affiliation":[{"name":"\u00c1rea de Microbiolog\u00eda, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, Campus de Vegazana, s\/n, 24071 Le\u00f3n, Spain"},{"name":"Instituto de Biotecnolog\u00eda de Le\u00f3n, INBIOTEC, Parque Cient\u00edfico de Le\u00f3n, 1 Av. 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Bioeng."},{"key":"2021112217202198900_B43","doi-asserted-by":"crossref","first-page":"2354","DOI":"10.1128\/jb.173.7.2354-2365.1991","article-title":"Characterization of the Cephalosporium acremonium pcbAB gene encoding \u03b1-aminoadiyl-cysteinyl-valine synthetase, a large multidomain peptide synthetase: linkage to the pcbC gene as a cluster of early cephalosporin-biosynthetic genes and evidence of multiple functional domains","volume":"173","author":"Guti\u00e9rrez","year":"1991","journal-title":"J. Bacteriol."},{"key":"2021112217202198900_B44","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1007\/BF02221518","article-title":"Autonomously replicating plasmids carrying the AMA1 region in Penicillium chrysogenum","volume":"29","author":"Fierro","year":"1996","journal-title":"Curr. 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