Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II
Thermolysin was used as a catalyst to obtain the following protected di‐ and tripeptide esters: Z‐Asn‐Leu‐OEt, Z‐Asn‐Phe‐OEt, Moz‐Asn‐Leu‐Gly‐OEt, Boc‐Asn‐Leu‐Gly‐OEt, Z‐Asn‐Leu‐Gly‐OEt, Moz‐Asn‐Leu‐Gly‐OBzl, Moz‐Asn‐Leu‐Gly‐OtBu, Moz‐Gln‐Leu‐Gly‐OEt, Moz‐Asn‐Ile‐Gly‐OEt, and Moz‐Asn‐Leu‐Ala‐OEt. Th...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1991-02, Vol.37 (2), p.128-133 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | MIRANDA, MARIA TERÊSA MACHINI TOMINAGA, MINEKO |
| description | Thermolysin was used as a catalyst to obtain the following protected di‐ and tripeptide esters: Z‐Asn‐Leu‐OEt, Z‐Asn‐Phe‐OEt, Moz‐Asn‐Leu‐Gly‐OEt, Boc‐Asn‐Leu‐Gly‐OEt, Z‐Asn‐Leu‐Gly‐OEt, Moz‐Asn‐Leu‐Gly‐OBzl, Moz‐Asn‐Leu‐Gly‐OtBu, Moz‐Gln‐Leu‐Gly‐OEt, Moz‐Asn‐Ile‐Gly‐OEt, and Moz‐Asn‐Leu‐Ala‐OEt. These compounds were obtained in pure form and the yields exceeded 50 %, except for Moz‐Asn‐Leu‐Gly‐OtBu and Boc‐Asn‐Leu‐Gly‐OEt. H‐Cys(Bz1)‐OtBu and H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 were both inadequate as amino components for obtaining Moz‐Asn‐Cys(Bz1)‐OtBu, Z‐Asn‐Cys(Bz1)‐OtBu and Moz‐Asn‐Cys(Bzl)‐Pro‐Leu‐Gly‐NH2 in the thermolysin‐catalyzed reactions. In the attempted synthesis of the protected pentapeptide amide, this protease cleaved the Pro‐Leu bond of the amino component H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 and catalyzed the coupling between the resulting dipeptide amide and Moz‐Asn‐OH, thus yielding Moz‐Asn‐Leu‐Gly‐NH2 as the main product. |
| doi_str_mv | 10.1111/j.1399-3011.1991.tb00092.x |
| format | Article |
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These compounds were obtained in pure form and the yields exceeded 50 %, except for Moz‐Asn‐Leu‐Gly‐OtBu and Boc‐Asn‐Leu‐Gly‐OEt. H‐Cys(Bz1)‐OtBu and H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 were both inadequate as amino components for obtaining Moz‐Asn‐Cys(Bz1)‐OtBu, Z‐Asn‐Cys(Bz1)‐OtBu and Moz‐Asn‐Cys(Bzl)‐Pro‐Leu‐Gly‐NH2 in the thermolysin‐catalyzed reactions. In the attempted synthesis of the protected pentapeptide amide, this protease cleaved the Pro‐Leu bond of the amino component H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 and catalyzed the coupling between the resulting dipeptide amide and Moz‐Asn‐OH, thus yielding Moz‐Asn‐Leu‐Gly‐NH2 as the main product.</description><identifier>ISSN: 0367-8377</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1111/j.1399-3011.1991.tb00092.x</identifier><identifier>PMID: 2019475</identifier><identifier>CODEN: IJPPC3</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Asparagine ; asparagine-containing peptides ; Biological and medical sciences ; Catalysis ; enzymatic syntheses ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrolases ; Molecular Sequence Data ; Oligopeptides - biosynthesis ; peptide syntheses ; thermolysin ; Thermolysin - metabolism</subject><ispartof>International Journal of Peptide and Protein Research, 1991-02, Vol.37 (2), p.128-133</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4378-ebbbe1e710fcd5cde0d1cb056dc1589f03da892349541b1f0ce63d3e64368f383</citedby><cites>FETCH-LOGICAL-c4378-ebbbe1e710fcd5cde0d1cb056dc1589f03da892349541b1f0ce63d3e64368f383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1399-3011.1991.tb00092.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1399-3011.1991.tb00092.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5075717$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2019475$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MIRANDA, MARIA TERÊSA MACHINI</creatorcontrib><creatorcontrib>TOMINAGA, MINEKO</creatorcontrib><title>Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II</title><title>International Journal of Peptide and Protein Research</title><addtitle>Int J Pept Protein Res</addtitle><description>Thermolysin was used as a catalyst to obtain the following protected di‐ and tripeptide esters: Z‐Asn‐Leu‐OEt, Z‐Asn‐Phe‐OEt, Moz‐Asn‐Leu‐Gly‐OEt, Boc‐Asn‐Leu‐Gly‐OEt, Z‐Asn‐Leu‐Gly‐OEt, Moz‐Asn‐Leu‐Gly‐OBzl, Moz‐Asn‐Leu‐Gly‐OtBu, Moz‐Gln‐Leu‐Gly‐OEt, Moz‐Asn‐Ile‐Gly‐OEt, and Moz‐Asn‐Leu‐Ala‐OEt. These compounds were obtained in pure form and the yields exceeded 50 %, except for Moz‐Asn‐Leu‐Gly‐OtBu and Boc‐Asn‐Leu‐Gly‐OEt. H‐Cys(Bz1)‐OtBu and H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 were both inadequate as amino components for obtaining Moz‐Asn‐Cys(Bz1)‐OtBu, Z‐Asn‐Cys(Bz1)‐OtBu and Moz‐Asn‐Cys(Bzl)‐Pro‐Leu‐Gly‐NH2 in the thermolysin‐catalyzed reactions. In the attempted synthesis of the protected pentapeptide amide, this protease cleaved the Pro‐Leu bond of the amino component H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 and catalyzed the coupling between the resulting dipeptide amide and Moz‐Asn‐OH, thus yielding Moz‐Asn‐Leu‐Gly‐NH2 as the main product.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Asparagine</subject><subject>asparagine-containing peptides</subject><subject>Biological and medical sciences</subject><subject>Catalysis</subject><subject>enzymatic syntheses</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolases</subject><subject>Molecular Sequence Data</subject><subject>Oligopeptides - biosynthesis</subject><subject>peptide syntheses</subject><subject>thermolysin</subject><subject>Thermolysin - metabolism</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMFu1DAQhi1EVZbCIyBFCHFL8MRxHHNB7BbalSpQpVY9Wo4zab0kThpnxYanx9FGe68vlj3f_B5_hHwEmkBYX3YJMCljRgESkBKSsaSUyjQ5vCKrU-k1WVGWi7hgQrwhb73fUcoyJtJzcp5SkJngK3J_94RD2zWTty7SPtKR0aMOxzEKF-j-Ta0erYn85MYn9NZHXR24Xg_60TqMTedGbZ11j1GP_Wgr9NF2-46c1brx-H7ZL8j9zx93m-v45vfVdvP9JjZhjiLGsiwRUACtTcVNhbQCU1KeVwZ4IWvKKl3IlGWSZ1BCTQ3mrGKYZywvalawC_L5mNsP3fMe_aha6w02jXbY7b0qKE9TDhDAr0fQDJ33A9aqH2yrh0kBVbNTtVOzODWLU7NTtThVh9D8YXllX7ZYnVoXiaH-aalrb3RTD9oZ608Yp4ILEAH7dsT-2ganFwygNuvLS0jn78bHBOtHPJwS9PBH5YIJrh5-Xal1dnst12uhBPsPAjyjhg</recordid><startdate>199102</startdate><enddate>199102</enddate><creator>MIRANDA, MARIA TERÊSA MACHINI</creator><creator>TOMINAGA, MINEKO</creator><general>Blackwell Publishing Ltd</general><general>Munksgaard</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>199102</creationdate><title>Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II</title><author>MIRANDA, MARIA TERÊSA MACHINI ; TOMINAGA, MINEKO</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4378-ebbbe1e710fcd5cde0d1cb056dc1589f03da892349541b1f0ce63d3e64368f383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Asparagine</topic><topic>asparagine-containing peptides</topic><topic>Biological and medical sciences</topic><topic>Catalysis</topic><topic>enzymatic syntheses</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolases</topic><topic>Molecular Sequence Data</topic><topic>Oligopeptides - biosynthesis</topic><topic>peptide syntheses</topic><topic>thermolysin</topic><topic>Thermolysin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MIRANDA, MARIA TERÊSA MACHINI</creatorcontrib><creatorcontrib>TOMINAGA, MINEKO</creatorcontrib><collection>Istex</collection><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>MEDLINE - Academic</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MIRANDA, MARIA TERÊSA MACHINI</au><au>TOMINAGA, MINEKO</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1991-02</date><risdate>1991</risdate><volume>37</volume><issue>2</issue><spage>128</spage><epage>133</epage><pages>128-133</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><coden>IJPPC3</coden><abstract>Thermolysin was used as a catalyst to obtain the following protected di‐ and tripeptide esters: Z‐Asn‐Leu‐OEt, Z‐Asn‐Phe‐OEt, Moz‐Asn‐Leu‐Gly‐OEt, Boc‐Asn‐Leu‐Gly‐OEt, Z‐Asn‐Leu‐Gly‐OEt, Moz‐Asn‐Leu‐Gly‐OBzl, Moz‐Asn‐Leu‐Gly‐OtBu, Moz‐Gln‐Leu‐Gly‐OEt, Moz‐Asn‐Ile‐Gly‐OEt, and Moz‐Asn‐Leu‐Ala‐OEt. These compounds were obtained in pure form and the yields exceeded 50 %, except for Moz‐Asn‐Leu‐Gly‐OtBu and Boc‐Asn‐Leu‐Gly‐OEt. H‐Cys(Bz1)‐OtBu and H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 were both inadequate as amino components for obtaining Moz‐Asn‐Cys(Bz1)‐OtBu, Z‐Asn‐Cys(Bz1)‐OtBu and Moz‐Asn‐Cys(Bzl)‐Pro‐Leu‐Gly‐NH2 in the thermolysin‐catalyzed reactions. In the attempted synthesis of the protected pentapeptide amide, this protease cleaved the Pro‐Leu bond of the amino component H‐Cys(Bz1)‐Pro‐Leu‐Gly‐NH2 and catalyzed the coupling between the resulting dipeptide amide and Moz‐Asn‐OH, thus yielding Moz‐Asn‐Leu‐Gly‐NH2 as the main product.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2019475</pmid><doi>10.1111/j.1399-3011.1991.tb00092.x</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Asparagine asparagine-containing peptides Biological and medical sciences Catalysis enzymatic syntheses Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Molecular Sequence Data Oligopeptides - biosynthesis peptide syntheses thermolysin Thermolysin - metabolism |
| title | Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II |
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