Characterization of the S Subsite Specificity of Cathepsin B
Five synthetic substrates containing different amino acid residues at the P 3 position (acetyl- X -Arg-Arg-AMC, where X is Gly, Glu, Arg, Val, and Tyr and where AMC represents 7-amido-4-methylcoumarin) were used to investigate the S 3 subsite specificity of cathepsin B. At pH 6.0, the specificity co...
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| Veröffentlicht in: | The Journal of biological chemistry 1995-07, Vol.270 (30), p.18036 |
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| container_issue | 30 |
| container_start_page | 18036 |
| container_title | The Journal of biological chemistry |
| container_volume | 270 |
| creator | Alpay Taralp Harvey Kaplan Iou-Iou Sytwu Isidoros Vlattas Regine Bohacek Anna K. Knap Tomoko Hirama Carol P. Huber Sadiq Hasnain |
| description | Five synthetic substrates containing different amino acid residues at the P 3 position (acetyl- X -Arg-Arg-AMC, where X is Gly, Glu, Arg, Val, and Tyr and where AMC represents 7-amido-4-methylcoumarin) were used to investigate the S 3 subsite specificity of cathepsin B. At pH 6.0, the specificity constant, k / K , for tripeptide substrate hydrolysis was observed to increase in the order Glu < Gly < Arg < Val < Tyr. Molecular modeling
studies of substrates containing a P 3 Glu, Arg, or Tyr covalently bound as the tetrahedral intermediate to the enzyme suggest that the specificity for a P 3 Tyr is because of a favorable aromatic-aromatic interaction with Tyr on the enzyme as well as a possible H bond between the P 3 Tyr hydroxyl and the side chain carboxyl of Asp . |
| doi_str_mv | 10.1074/jbc.270.30.18036 |
| format | Article |
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studies of substrates containing a P 3 Glu, Arg, or Tyr covalently bound as the tetrahedral intermediate to the enzyme suggest that the specificity for a P 3 Tyr is because of a favorable aromatic-aromatic interaction with Tyr on the enzyme as well as a possible H bond between the P 3 Tyr hydroxyl and the side chain carboxyl of Asp .</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.30.18036</identifier><identifier>PMID: 7629112</identifier><language>eng</language><publisher>American Society for Biochemistry and Molecular Biology</publisher><ispartof>The Journal of biological chemistry, 1995-07, Vol.270 (30), p.18036</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Alpay Taralp</creatorcontrib><creatorcontrib>Harvey Kaplan</creatorcontrib><creatorcontrib>Iou-Iou Sytwu</creatorcontrib><creatorcontrib>Isidoros Vlattas</creatorcontrib><creatorcontrib>Regine Bohacek</creatorcontrib><creatorcontrib>Anna K. Knap</creatorcontrib><creatorcontrib>Tomoko Hirama</creatorcontrib><creatorcontrib>Carol P. Huber</creatorcontrib><creatorcontrib>Sadiq Hasnain</creatorcontrib><title>Characterization of the S Subsite Specificity of Cathepsin B</title><title>The Journal of biological chemistry</title><description>Five synthetic substrates containing different amino acid residues at the P 3 position (acetyl- X -Arg-Arg-AMC, where X is Gly, Glu, Arg, Val, and Tyr and where AMC represents 7-amido-4-methylcoumarin) were used to investigate the S 3 subsite specificity of cathepsin B. At pH 6.0, the specificity constant, k / K , for tripeptide substrate hydrolysis was observed to increase in the order Glu < Gly < Arg < Val < Tyr. Molecular modeling
studies of substrates containing a P 3 Glu, Arg, or Tyr covalently bound as the tetrahedral intermediate to the enzyme suggest that the specificity for a P 3 Tyr is because of a favorable aromatic-aromatic interaction with Tyr on the enzyme as well as a possible H bond between the P 3 Tyr hydroxyl and the side chain carboxyl of Asp .</description><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqNjj9vwjAUxJ9QEYQ_O6OHrgnPNiGJ1KlRETsMbJFjOfhFQFBshMqnx6B-gN5yd_rdcAALjgnHbLVsa52IDBMZeo5yPYCIYy5jmfLDB0SIgseFSPMxTJxrMWhV8BGMsrUoOBcRfJVW9Up709NDeeourGuYt4bt2O5WO_IhXY2mhjT53xcsVcBXRxf2PYNho07OzP98Cp-bn325jS0d7Z16U9XUaWvOVfhYSazeH-U_Z08Vjz8j</recordid><startdate>19950728</startdate><enddate>19950728</enddate><creator>Alpay Taralp</creator><creator>Harvey Kaplan</creator><creator>Iou-Iou Sytwu</creator><creator>Isidoros Vlattas</creator><creator>Regine Bohacek</creator><creator>Anna K. Knap</creator><creator>Tomoko Hirama</creator><creator>Carol P. Huber</creator><creator>Sadiq Hasnain</creator><general>American Society for Biochemistry and Molecular Biology</general><scope/></search><sort><creationdate>19950728</creationdate><title>Characterization of the S Subsite Specificity of Cathepsin B</title><author>Alpay Taralp ; Harvey Kaplan ; Iou-Iou Sytwu ; Isidoros Vlattas ; Regine Bohacek ; Anna K. Knap ; Tomoko Hirama ; Carol P. Huber ; Sadiq Hasnain</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-highwire_biochem_270_30_180363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alpay Taralp</creatorcontrib><creatorcontrib>Harvey Kaplan</creatorcontrib><creatorcontrib>Iou-Iou Sytwu</creatorcontrib><creatorcontrib>Isidoros Vlattas</creatorcontrib><creatorcontrib>Regine Bohacek</creatorcontrib><creatorcontrib>Anna K. Knap</creatorcontrib><creatorcontrib>Tomoko Hirama</creatorcontrib><creatorcontrib>Carol P. Huber</creatorcontrib><creatorcontrib>Sadiq Hasnain</creatorcontrib><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alpay Taralp</au><au>Harvey Kaplan</au><au>Iou-Iou Sytwu</au><au>Isidoros Vlattas</au><au>Regine Bohacek</au><au>Anna K. Knap</au><au>Tomoko Hirama</au><au>Carol P. Huber</au><au>Sadiq Hasnain</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the S Subsite Specificity of Cathepsin B</atitle><jtitle>The Journal of biological chemistry</jtitle><date>1995-07-28</date><risdate>1995</risdate><volume>270</volume><issue>30</issue><spage>18036</spage><pages>18036-</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Five synthetic substrates containing different amino acid residues at the P 3 position (acetyl- X -Arg-Arg-AMC, where X is Gly, Glu, Arg, Val, and Tyr and where AMC represents 7-amido-4-methylcoumarin) were used to investigate the S 3 subsite specificity of cathepsin B. At pH 6.0, the specificity constant, k / K , for tripeptide substrate hydrolysis was observed to increase in the order Glu < Gly < Arg < Val < Tyr. Molecular modeling
studies of substrates containing a P 3 Glu, Arg, or Tyr covalently bound as the tetrahedral intermediate to the enzyme suggest that the specificity for a P 3 Tyr is because of a favorable aromatic-aromatic interaction with Tyr on the enzyme as well as a possible H bond between the P 3 Tyr hydroxyl and the side chain carboxyl of Asp .</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7629112</pmid><doi>10.1074/jbc.270.30.18036</doi></addata></record> |
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| ispartof | The Journal of biological chemistry, 1995-07, Vol.270 (30), p.18036 |
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| language | eng |
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| title | Characterization of the S Subsite Specificity of Cathepsin B |
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