Salt-Enhanced Aminolysis of Acyl-α-Chymotrypsins by Dipeptides
Increase in KC1 concentration from 0.1 m to 3 m enhances the chymotrypsin-catalyzed acyl-transfer to a series of dipeptides, H2N-CH(R1)C(O)NHCH(R2)C(O)O, by factors between 15 and 44. The observed positive salt effect seems to be a screening of the unfavorable electrostatic interaction between the d...
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| Veröffentlicht in: | Biocatalysis 1991, Vol.4 (4), p.291-296 |
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| container_title | Biocatalysis |
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| creator | Schellenberger, V. Aaviksaar, A. Jakubke, H.-D. |
| description | Increase in KC1 concentration from 0.1 m to 3 m enhances the chymotrypsin-catalyzed acyl-transfer to a series of dipeptides, H2N-CH(R1)C(O)NHCH(R2)C(O)O, by factors between 15 and 44. The observed positive salt effect seems to be a screening of the unfavorable electrostatic interaction between the dipeptide carboxyl group and a negatively charged area in the S' subsite on the enzyme surface. The effect is of practical use in preparative peptide synthesis-in 3 m KCl solutions the analytical yields of tripeptides of up to 99 per cent have been obtained. |
| doi_str_mv | 10.3109/10242429109000692 |
| format | Article |
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The observed positive salt effect seems to be a screening of the unfavorable electrostatic interaction between the dipeptide carboxyl group and a negatively charged area in the S' subsite on the enzyme surface. The effect is of practical use in preparative peptide synthesis-in 3 m KCl solutions the analytical yields of tripeptides of up to 99 per cent have been obtained.</description><identifier>ISSN: 1024-2422</identifier><identifier>ISSN: 0886-4454</identifier><identifier>EISSN: 1029-2446</identifier><identifier>DOI: 10.3109/10242429109000692</identifier><language>eng</language><publisher>Yverdon: Informa UK Ltd</publisher><subject>acyl transfer ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; dipeptide nucleophiles ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. 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The observed positive salt effect seems to be a screening of the unfavorable electrostatic interaction between the dipeptide carboxyl group and a negatively charged area in the S' subsite on the enzyme surface. The effect is of practical use in preparative peptide synthesis-in 3 m KCl solutions the analytical yields of tripeptides of up to 99 per cent have been obtained.</description><subject>acyl transfer</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>dipeptide nucleophiles</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolases</subject><subject>positive salt effect</subject><subject>α-chymotrypsin</subject><issn>1024-2422</issn><issn>0886-4454</issn><issn>1029-2446</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNp9kMtKxDAUhoMoOI4-gLtuXFZz6yUoyDCOFxhwoa5LmiY0Q9qUpCJ5LF_EZzJjFRFhOIvzczjfufwAnCJ4ThBkFwhiGoNFDSHMGd4Ds1hjKaY03__SNGqMD8GR9xsIEcGsmIHrJ27GdNW3vBeySRad7q0JXvvEqmQhgkk_3tNlGzo7ujB43fukDsmNHuQw6kb6Y3CguPHy5DvPwcvt6nl5n64f7x6Wi3UqMCNjynPGaY2EUHXBsKISFwxmOVRNSUteKt7AMkdKykw1gsqCiDxHvKhhJgSkWJI5QNNc4az3TqpqcLrjLlQIVlsHqn8OROZsYgbuBTfKxR-1_wVZkRFEt31XU5_ulXUdf7PONNXIg7HuByK71lz-wVsZLW0Fd7La2FfXR1t2HPkJI1mBGA</recordid><startdate>1991</startdate><enddate>1991</enddate><creator>Schellenberger, V.</creator><creator>Aaviksaar, A.</creator><creator>Jakubke, H.-D.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><general>Harwood Academic Publishers</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>1991</creationdate><title>Salt-Enhanced Aminolysis of Acyl-α-Chymotrypsins by Dipeptides</title><author>Schellenberger, V. ; Aaviksaar, A. ; Jakubke, H.-D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c293t-a69a4b1ccfb792f4e2790560fd848a8fad0861fee5fdc4e73c661a7b05cc042e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>acyl transfer</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>dipeptide nucleophiles</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolases</topic><topic>positive salt effect</topic><topic>α-chymotrypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schellenberger, V.</creatorcontrib><creatorcontrib>Aaviksaar, A.</creatorcontrib><creatorcontrib>Jakubke, H.-D.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Biocatalysis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schellenberger, V.</au><au>Aaviksaar, A.</au><au>Jakubke, H.-D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Salt-Enhanced Aminolysis of Acyl-α-Chymotrypsins by Dipeptides</atitle><jtitle>Biocatalysis</jtitle><date>1991</date><risdate>1991</risdate><volume>4</volume><issue>4</issue><spage>291</spage><epage>296</epage><pages>291-296</pages><issn>1024-2422</issn><issn>0886-4454</issn><eissn>1029-2446</eissn><abstract>Increase in KC1 concentration from 0.1 m to 3 m enhances the chymotrypsin-catalyzed acyl-transfer to a series of dipeptides, H2N-CH(R1)C(O)NHCH(R2)C(O)O, by factors between 15 and 44. The observed positive salt effect seems to be a screening of the unfavorable electrostatic interaction between the dipeptide carboxyl group and a negatively charged area in the S' subsite on the enzyme surface. The effect is of practical use in preparative peptide synthesis-in 3 m KCl solutions the analytical yields of tripeptides of up to 99 per cent have been obtained.</abstract><cop>Yverdon</cop><pub>Informa UK Ltd</pub><doi>10.3109/10242429109000692</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biocatalysis, 1991, Vol.4 (4), p.291-296 |
| issn | 1024-2422 0886-4454 1029-2446 |
| language | eng |
| recordid | cdi_informahealthcare_journals_10_3109_10242429109000692 |
| source | Taylor & Francis |
| subjects | acyl transfer Analytical, structural and metabolic biochemistry Biological and medical sciences dipeptide nucleophiles Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases positive salt effect α-chymotrypsin |
| title | Salt-Enhanced Aminolysis of Acyl-α-Chymotrypsins by Dipeptides |
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