Substrate Specificity of Penicillin Acylase from Streptomyces lavendulae
The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicilli...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2002-03, Vol.291 (3), p.593-597 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Torres-Guzmán, Raquel de la Mata, Isabel Torres-Bacete, Jesús Arroyo, Miguel Castillón, Marı́a Pilar Acebal, Carmen |
| description | The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicillin K (octanoyl penicillin) with a kcat/Km of 165.3 mM−1 s−1. The enzyme hydrolyses also chromogenic substrates as NIPOAB (2-nitro-5-phenoxyacetamido benzoic acid), NIHAB (2-nitro-5-hexanoylamido benzoic acid) or NIOAB (2-nitro-5-octanoylamido benzoic acid), however failed to hydrolyse phenylacetil penicillin (penicillin G) or NIPAB (2-nitro-5-phenylacetamido benzoic acid) and penicillins with polar substituents in the acyl moiety. These results suggest that the structure of the acyl moiety of the substrate is more determinant than the amino moiety for enzyme specificity. The enzyme was inhibited by several organic acids and the extent of inhibition changed with the hydrophobicity of the acid. The best inhibitor was octanoic acid with a Ki of 0.8 mM. All the results, taking together, point to an active site highly hydrophobic for this penicillin acylase from Streptomyces lavendulae. |
| doi_str_mv | 10.1006/bbrc.2002.6485 |
| format | Article |
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The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicillin K (octanoyl penicillin) with a kcat/Km of 165.3 mM−1 s−1. The enzyme hydrolyses also chromogenic substrates as NIPOAB (2-nitro-5-phenoxyacetamido benzoic acid), NIHAB (2-nitro-5-hexanoylamido benzoic acid) or NIOAB (2-nitro-5-octanoylamido benzoic acid), however failed to hydrolyse phenylacetil penicillin (penicillin G) or NIPAB (2-nitro-5-phenylacetamido benzoic acid) and penicillins with polar substituents in the acyl moiety. These results suggest that the structure of the acyl moiety of the substrate is more determinant than the amino moiety for enzyme specificity. The enzyme was inhibited by several organic acids and the extent of inhibition changed with the hydrophobicity of the acid. The best inhibitor was octanoic acid with a Ki of 0.8 mM. All the results, taking together, point to an active site highly hydrophobic for this penicillin acylase from Streptomyces lavendulae.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2002.6485</identifier><identifier>PMID: 11855830</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Chromogenic Compounds - chemistry ; Chromogenic Compounds - metabolism ; chromogenic substrates ; enzyme specificity ; Kinetics ; Models, Chemical ; penicillin ; penicillin acylase ; Penicillin Amidase - metabolism ; Penicillin V - chemistry ; Penicillin V - metabolism ; Penicillins - chemistry ; Penicillins - metabolism ; Streptomyces - enzymology ; Streptomyces lavendulae ; Substrate Specificity</subject><ispartof>Biochemical and biophysical research communications, 2002-03, Vol.291 (3), p.593-597</ispartof><rights>2002 Elsevier Science (USA)</rights><rights>2002 Elsevier Science (USA).</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-627089e1857b00c4b752cfc24a8c0ab1d67774182bea9e19d9414b459a17ff133</citedby><cites>FETCH-LOGICAL-c340t-627089e1857b00c4b752cfc24a8c0ab1d67774182bea9e19d9414b459a17ff133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2002.6485$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11855830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Torres-Guzmán, Raquel</creatorcontrib><creatorcontrib>de la Mata, Isabel</creatorcontrib><creatorcontrib>Torres-Bacete, Jesús</creatorcontrib><creatorcontrib>Arroyo, Miguel</creatorcontrib><creatorcontrib>Castillón, Marı́a Pilar</creatorcontrib><creatorcontrib>Acebal, Carmen</creatorcontrib><title>Substrate Specificity of Penicillin Acylase from Streptomyces lavendulae</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicillin K (octanoyl penicillin) with a kcat/Km of 165.3 mM−1 s−1. The enzyme hydrolyses also chromogenic substrates as NIPOAB (2-nitro-5-phenoxyacetamido benzoic acid), NIHAB (2-nitro-5-hexanoylamido benzoic acid) or NIOAB (2-nitro-5-octanoylamido benzoic acid), however failed to hydrolyse phenylacetil penicillin (penicillin G) or NIPAB (2-nitro-5-phenylacetamido benzoic acid) and penicillins with polar substituents in the acyl moiety. These results suggest that the structure of the acyl moiety of the substrate is more determinant than the amino moiety for enzyme specificity. The enzyme was inhibited by several organic acids and the extent of inhibition changed with the hydrophobicity of the acid. The best inhibitor was octanoic acid with a Ki of 0.8 mM. All the results, taking together, point to an active site highly hydrophobic for this penicillin acylase from Streptomyces lavendulae.</description><subject>Chromogenic Compounds - chemistry</subject><subject>Chromogenic Compounds - metabolism</subject><subject>chromogenic substrates</subject><subject>enzyme specificity</subject><subject>Kinetics</subject><subject>Models, Chemical</subject><subject>penicillin</subject><subject>penicillin acylase</subject><subject>Penicillin Amidase - metabolism</subject><subject>Penicillin V - chemistry</subject><subject>Penicillin V - metabolism</subject><subject>Penicillins - chemistry</subject><subject>Penicillins - metabolism</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces lavendulae</subject><subject>Substrate Specificity</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1LxDAQhoMo7rp69Sg9ees6adOmPS6LusKCwip4C0k6gUi_TFKh_96WXfDkaebwzDu8DyG3FNYUIH9Qyul1ApCsc1ZkZ2RJoYQ4ocDOyRImIk5K-rkgV95_AVDK8vKSLCgtsqxIYUl2h0H54GTA6NCjtsZqG8aoM9EbttNe17aNNnqspcfIuK6JDsFhH7pm1OijWv5gWw21xGtyYWTt8eY0V-Tj6fF9u4v3r88v280-1imDEOcJh6LE6T9XAJopniXa6ITJQoNUtMo554wWiUI5YWVVMsoUy0pJuTE0TVfk_pjbu-57QB9EY73GupYtdoMXfKrIgc3g-ghq13nv0Ije2Ua6UVAQszsxuxOzOzG7mw7uTsmDarD6w0-yJqA4Ajj1-7HohNcWW42VdaiDqDr7X_YvQJB9gA</recordid><startdate>20020301</startdate><enddate>20020301</enddate><creator>Torres-Guzmán, Raquel</creator><creator>de la Mata, Isabel</creator><creator>Torres-Bacete, Jesús</creator><creator>Arroyo, Miguel</creator><creator>Castillón, Marı́a Pilar</creator><creator>Acebal, Carmen</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020301</creationdate><title>Substrate Specificity of Penicillin Acylase from Streptomyces lavendulae</title><author>Torres-Guzmán, Raquel ; de la Mata, Isabel ; Torres-Bacete, Jesús ; Arroyo, Miguel ; Castillón, Marı́a Pilar ; Acebal, Carmen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-627089e1857b00c4b752cfc24a8c0ab1d67774182bea9e19d9414b459a17ff133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Chromogenic Compounds - chemistry</topic><topic>Chromogenic Compounds - metabolism</topic><topic>chromogenic substrates</topic><topic>enzyme specificity</topic><topic>Kinetics</topic><topic>Models, Chemical</topic><topic>penicillin</topic><topic>penicillin acylase</topic><topic>Penicillin Amidase - metabolism</topic><topic>Penicillin V - chemistry</topic><topic>Penicillin V - metabolism</topic><topic>Penicillins - chemistry</topic><topic>Penicillins - metabolism</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces lavendulae</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Torres-Guzmán, Raquel</creatorcontrib><creatorcontrib>de la Mata, Isabel</creatorcontrib><creatorcontrib>Torres-Bacete, Jesús</creatorcontrib><creatorcontrib>Arroyo, Miguel</creatorcontrib><creatorcontrib>Castillón, Marı́a Pilar</creatorcontrib><creatorcontrib>Acebal, Carmen</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Torres-Guzmán, Raquel</au><au>de la Mata, Isabel</au><au>Torres-Bacete, Jesús</au><au>Arroyo, Miguel</au><au>Castillón, Marı́a Pilar</au><au>Acebal, Carmen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate Specificity of Penicillin Acylase from Streptomyces lavendulae</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2002-03-01</date><risdate>2002</risdate><volume>291</volume><issue>3</issue><spage>593</spage><epage>597</epage><pages>593-597</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicillin K (octanoyl penicillin) with a kcat/Km of 165.3 mM−1 s−1. The enzyme hydrolyses also chromogenic substrates as NIPOAB (2-nitro-5-phenoxyacetamido benzoic acid), NIHAB (2-nitro-5-hexanoylamido benzoic acid) or NIOAB (2-nitro-5-octanoylamido benzoic acid), however failed to hydrolyse phenylacetil penicillin (penicillin G) or NIPAB (2-nitro-5-phenylacetamido benzoic acid) and penicillins with polar substituents in the acyl moiety. These results suggest that the structure of the acyl moiety of the substrate is more determinant than the amino moiety for enzyme specificity. The enzyme was inhibited by several organic acids and the extent of inhibition changed with the hydrophobicity of the acid. The best inhibitor was octanoic acid with a Ki of 0.8 mM. All the results, taking together, point to an active site highly hydrophobic for this penicillin acylase from Streptomyces lavendulae.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11855830</pmid><doi>10.1006/bbrc.2002.6485</doi><tpages>5</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Chromogenic Compounds - chemistry Chromogenic Compounds - metabolism chromogenic substrates enzyme specificity Kinetics Models, Chemical penicillin penicillin acylase Penicillin Amidase - metabolism Penicillin V - chemistry Penicillin V - metabolism Penicillins - chemistry Penicillins - metabolism Streptomyces - enzymology Streptomyces lavendulae Substrate Specificity |
| title | Substrate Specificity of Penicillin Acylase from Streptomyces lavendulae |
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