SNA-60-367 Components, New Peptide Enzyme Inhibitors of Aromatase: Structure of the Fatty Acid Side Chain and Amino Acid Sequence by Mass Spectrometry
SNA-60-367 components, new peptide enzyme inhibitors of aromatase, were isolated from the culture broth of soil bacterium, Bacillus sp. SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid s...
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| Veröffentlicht in: | Journal of antibiotics 2003/08/25, Vol.56(8), pp.716-720 |
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| creator | ESUMI, YASUAKI SUZUKI, YOSHIKATSU ITOH, YUMIKO CHIJIMATSU, MASAO URAMOTO, MASAKAZU KIMURA, KEN-ICHI NAKAYAMA, SHOJI YOSHIHAMA, MAKOTO ICHIKAWA, TERUO HARAMO, TOYOHIRO FUJISHIGE, JIROU |
| description | SNA-60-367 components, new peptide enzyme inhibitors of aromatase, were isolated from the culture broth of soil bacterium, Bacillus sp. SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid side chain. The structures of the fatty acid moieties were shown to be (3-hydroxy)heptadecanoic acid and (3-hydroxy)hexadecanoic acid that possess normal-, iso- or anteiso-type alkyl groups. The amino acid sequence of the open form of the lactone ring of the acylpeptides is RCO-L-Glu-D-Orn-L(or D)-Tyr3-D-allo-Thr-L-Glu-D-X1 (Ala, Aba or Val)-L-Pro-L-Gln-D(or L)-Tyr-L-X102(Ile or Val)-OH. The lactone ring of SNA-60-367 components is formed between Tyr3 and X102. |
| doi_str_mv | 10.7164/antibiotics.56.716 |
| format | Article |
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SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid side chain. The structures of the fatty acid moieties were shown to be (3-hydroxy)heptadecanoic acid and (3-hydroxy)hexadecanoic acid that possess normal-, iso- or anteiso-type alkyl groups. The amino acid sequence of the open form of the lactone ring of the acylpeptides is RCO-L-Glu-D-Orn-L(or D)-Tyr3-D-allo-Thr-L-Glu-D-X1 (Ala, Aba or Val)-L-Pro-L-Gln-D(or L)-Tyr-L-X102(Ile or Val)-OH. The lactone ring of SNA-60-367 components is formed between Tyr3 and X102.</description><identifier>ISSN: 0021-8820</identifier><identifier>EISSN: 1881-1469</identifier><identifier>DOI: 10.7164/antibiotics.56.716</identifier><identifier>PMID: 14563162</identifier><identifier>CODEN: JANTAJ</identifier><language>eng</language><publisher>Tokyo: JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</publisher><subject>Aromatase Inhibitors ; Bacillus ; Biological and medical sciences ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - isolation & purification ; Enzyme Inhibitors - pharmacology ; Hormones. Endocrine system ; Mass Spectrometry ; Medical sciences ; Oligopeptides - chemistry ; Oligopeptides - isolation & purification ; Oligopeptides - pharmacology ; Pharmacology. Drug treatments ; Structure-Activity Relationship</subject><ispartof>The Journal of Antibiotics, 2003/08/25, Vol.56(8), pp.716-720</ispartof><rights>Japan Antibiotics Research Association</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c668t-feb99382199b0744decfd9fcbe18cab97ff3862709368b0a0beb6af3de4685bb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15166916$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14563162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ESUMI, YASUAKI</creatorcontrib><creatorcontrib>SUZUKI, YOSHIKATSU</creatorcontrib><creatorcontrib>ITOH, YUMIKO</creatorcontrib><creatorcontrib>CHIJIMATSU, MASAO</creatorcontrib><creatorcontrib>URAMOTO, MASAKAZU</creatorcontrib><creatorcontrib>KIMURA, KEN-ICHI</creatorcontrib><creatorcontrib>NAKAYAMA, SHOJI</creatorcontrib><creatorcontrib>YOSHIHAMA, MAKOTO</creatorcontrib><creatorcontrib>ICHIKAWA, TERUO</creatorcontrib><creatorcontrib>HARAMO, TOYOHIRO</creatorcontrib><creatorcontrib>FUJISHIGE, JIROU</creatorcontrib><title>SNA-60-367 Components, New Peptide Enzyme Inhibitors of Aromatase: Structure of the Fatty Acid Side Chain and Amino Acid Sequence by Mass Spectrometry</title><title>Journal of antibiotics</title><addtitle>J. Antibiot.</addtitle><description>SNA-60-367 components, new peptide enzyme inhibitors of aromatase, were isolated from the culture broth of soil bacterium, Bacillus sp. SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid side chain. The structures of the fatty acid moieties were shown to be (3-hydroxy)heptadecanoic acid and (3-hydroxy)hexadecanoic acid that possess normal-, iso- or anteiso-type alkyl groups. The amino acid sequence of the open form of the lactone ring of the acylpeptides is RCO-L-Glu-D-Orn-L(or D)-Tyr3-D-allo-Thr-L-Glu-D-X1 (Ala, Aba or Val)-L-Pro-L-Gln-D(or L)-Tyr-L-X102(Ile or Val)-OH. The lactone ring of SNA-60-367 components is formed between Tyr3 and X102.</description><subject>Aromatase Inhibitors</subject><subject>Bacillus</subject><subject>Biological and medical sciences</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - isolation & purification</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Hormones. Endocrine system</subject><subject>Mass Spectrometry</subject><subject>Medical sciences</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - isolation & purification</subject><subject>Oligopeptides - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Structure-Activity Relationship</subject><issn>0021-8820</issn><issn>1881-1469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EotPCC7BA3sCqKXZ-_MMuGrVQUQrSwDqynRvGVWIPtiMUHoTnJWGitjs2tnTvd8850kHoFSUXnLLynXLJauuTNfGiYsvsCdpQIWhGSyafog0hOc2EyMkJOo3xjpCCF1w8Rye0rFhBWb5Bf3a3dcZIVjCOt344eAcuxXN8C7_wVzgk2wK-dL-nAfC12892yYeIfYfr4AeVVIT3eJfCaNIYYJmnPeArldKEa2NbvFsEtntlHVauxfVgnV838HMEZwDrCX9WMeLdAUyaVSGF6QV61qk-wsv1P0Pfry6_bT9mN18-XG_rm8wwJlLWgZayEDmVUhNeli2YrpWd0UCFUVryrisEyzmRBROaKKJBM9UVLZRMVFoXZ-jtUfcQ_Bwnpmaw0UDfKwd-jA2nuaxImf8XpJyTOVI1g_kRNMHHGKBrDsEOKkwNJc1SW_OotqZiy2w-er2qj3qA9uFk7WkG3qyAikb1XVDO2PjAVZQx-U_o05G7i0n9gHtAhdmuh8feVDKx-K_PHOOeMnsVGnDFXz68v6M</recordid><startdate>20030801</startdate><enddate>20030801</enddate><creator>ESUMI, YASUAKI</creator><creator>SUZUKI, YOSHIKATSU</creator><creator>ITOH, YUMIKO</creator><creator>CHIJIMATSU, MASAO</creator><creator>URAMOTO, MASAKAZU</creator><creator>KIMURA, KEN-ICHI</creator><creator>NAKAYAMA, SHOJI</creator><creator>YOSHIHAMA, MAKOTO</creator><creator>ICHIKAWA, TERUO</creator><creator>HARAMO, TOYOHIRO</creator><creator>FUJISHIGE, JIROU</creator><general>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</general><general>Japan Antibiotics Research Association</general><scope>IQODW</scope><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>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20030801</creationdate><title>SNA-60-367 Components, New Peptide Enzyme Inhibitors of Aromatase: Structure of the Fatty Acid Side Chain and Amino Acid Sequence by Mass Spectrometry</title><author>ESUMI, YASUAKI ; SUZUKI, YOSHIKATSU ; ITOH, YUMIKO ; CHIJIMATSU, MASAO ; URAMOTO, MASAKAZU ; KIMURA, KEN-ICHI ; NAKAYAMA, SHOJI ; YOSHIHAMA, MAKOTO ; ICHIKAWA, TERUO ; HARAMO, TOYOHIRO ; FUJISHIGE, JIROU</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c668t-feb99382199b0744decfd9fcbe18cab97ff3862709368b0a0beb6af3de4685bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aromatase Inhibitors</topic><topic>Bacillus</topic><topic>Biological and medical sciences</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - isolation & purification</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Hormones. Endocrine system</topic><topic>Mass Spectrometry</topic><topic>Medical sciences</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - isolation & purification</topic><topic>Oligopeptides - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ESUMI, YASUAKI</creatorcontrib><creatorcontrib>SUZUKI, YOSHIKATSU</creatorcontrib><creatorcontrib>ITOH, YUMIKO</creatorcontrib><creatorcontrib>CHIJIMATSU, MASAO</creatorcontrib><creatorcontrib>URAMOTO, MASAKAZU</creatorcontrib><creatorcontrib>KIMURA, KEN-ICHI</creatorcontrib><creatorcontrib>NAKAYAMA, SHOJI</creatorcontrib><creatorcontrib>YOSHIHAMA, MAKOTO</creatorcontrib><creatorcontrib>ICHIKAWA, TERUO</creatorcontrib><creatorcontrib>HARAMO, TOYOHIRO</creatorcontrib><creatorcontrib>FUJISHIGE, JIROU</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of antibiotics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ESUMI, YASUAKI</au><au>SUZUKI, YOSHIKATSU</au><au>ITOH, YUMIKO</au><au>CHIJIMATSU, MASAO</au><au>URAMOTO, MASAKAZU</au><au>KIMURA, KEN-ICHI</au><au>NAKAYAMA, SHOJI</au><au>YOSHIHAMA, MAKOTO</au><au>ICHIKAWA, TERUO</au><au>HARAMO, TOYOHIRO</au><au>FUJISHIGE, JIROU</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SNA-60-367 Components, New Peptide Enzyme Inhibitors of Aromatase: Structure of the Fatty Acid Side Chain and Amino Acid Sequence by Mass Spectrometry</atitle><jtitle>Journal of antibiotics</jtitle><addtitle>J. Antibiot.</addtitle><date>2003-08-01</date><risdate>2003</risdate><volume>56</volume><issue>8</issue><spage>716</spage><epage>720</epage><pages>716-720</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><coden>JANTAJ</coden><abstract>SNA-60-367 components, new peptide enzyme inhibitors of aromatase, were isolated from the culture broth of soil bacterium, Bacillus sp. SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid side chain. The structures of the fatty acid moieties were shown to be (3-hydroxy)heptadecanoic acid and (3-hydroxy)hexadecanoic acid that possess normal-, iso- or anteiso-type alkyl groups. The amino acid sequence of the open form of the lactone ring of the acylpeptides is RCO-L-Glu-D-Orn-L(or D)-Tyr3-D-allo-Thr-L-Glu-D-X1 (Ala, Aba or Val)-L-Pro-L-Gln-D(or L)-Tyr-L-X102(Ile or Val)-OH. The lactone ring of SNA-60-367 components is formed between Tyr3 and X102.</abstract><cop>Tokyo</cop><pub>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</pub><pmid>14563162</pmid><doi>10.7164/antibiotics.56.716</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-8820 |
| ispartof | The Journal of Antibiotics, 2003/08/25, Vol.56(8), pp.716-720 |
| issn | 0021-8820 1881-1469 |
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| subjects | Aromatase Inhibitors Bacillus Biological and medical sciences Enzyme Inhibitors - chemistry Enzyme Inhibitors - isolation & purification Enzyme Inhibitors - pharmacology Hormones. Endocrine system Mass Spectrometry Medical sciences Oligopeptides - chemistry Oligopeptides - isolation & purification Oligopeptides - pharmacology Pharmacology. Drug treatments Structure-Activity Relationship |
| title | SNA-60-367 Components, New Peptide Enzyme Inhibitors of Aromatase: Structure of the Fatty Acid Side Chain and Amino Acid Sequence by Mass Spectrometry |
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