Inhibition of the aspartic proteinase from HIV-2
Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from th...
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| Veröffentlicht in: | FEBS letters 1989-08, Vol.253 (1), p.214-216 |
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| container_title | FEBS letters |
| container_volume | 253 |
| creator | Richards, Anthony D. Broadhurst, Anne V. Ritchie, Alison J. Dunn, Ben M. Kay, John |
| description | Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus. |
| doi_str_mv | 10.1016/0014-5793(89)80961-5 |
| format | Article |
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Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(89)80961-5</identifier><identifier>PMID: 2668032</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Acetyl-pepstatin ; AIDS/HIV ; Analytical, structural and metabolic biochemistry ; Aspartic Acid Endopeptidases ; Biological and medical sciences ; Endopeptidases ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; HIV, human immunodeficiency virus ; HIV-1 proteinase ; HIV-2 - enzymology ; HIV-2 proteinase ; Hydrogen-Ion Concentration ; Hydrolases ; Iva, isovaleryl ; Kinetics ; Molecular Weight ; Protease Inhibitors - pharmacology ; Renin inhibitor, H-261 ; Sta, 4-amino-3-hydroxy-6-methylheptanoic acid ; Substrate Specificity ; the in the sequence containing PhePro indicates the scissile peptide bond in the substrate ; Tight binding inhibitor</subject><ispartof>FEBS letters, 1989-08, Vol.253 (1), p.214-216</ispartof><rights>1989</rights><rights>FEBS Letters 253 (1989) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5275-afbdb997669c69a2307dbe1312d8f34e1db650326d1dc292ca1d87ed88b967213</citedby><cites>FETCH-LOGICAL-c5275-afbdb997669c69a2307dbe1312d8f34e1db650326d1dc292ca1d87ed88b967213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(89)80961-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19420107$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2668032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richards, Anthony D.</creatorcontrib><creatorcontrib>Broadhurst, Anne V.</creatorcontrib><creatorcontrib>Ritchie, Alison J.</creatorcontrib><creatorcontrib>Dunn, Ben M.</creatorcontrib><creatorcontrib>Kay, John</creatorcontrib><title>Inhibition of the aspartic proteinase from HIV-2</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.</description><subject>Acetyl-pepstatin</subject><subject>AIDS/HIV</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Aspartic Acid Endopeptidases</subject><subject>Biological and medical sciences</subject><subject>Endopeptidases</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HIV, human immunodeficiency virus</subject><subject>HIV-1 proteinase</subject><subject>HIV-2 - enzymology</subject><subject>HIV-2 proteinase</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Iva, isovaleryl</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Renin inhibitor, H-261</subject><subject>Sta, 4-amino-3-hydroxy-6-methylheptanoic acid</subject><subject>Substrate Specificity</subject><subject>the in the sequence containing PhePro indicates the scissile peptide bond in the substrate</subject><subject>Tight binding inhibitor</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1O3DAUha2qiA7QN2ilbFrBIq2vHf9tkFrEwEhI3ZRuLce-EUaZZGpnqHj7OswIdi0ry_ece3z8EfIB6BegIL9SCk0tlOGn2pxpaiTU4g1ZgFa85o3Ub8ni2fKOHOV8T8tdgzkkh0xKTTlbELoa7mIbpzgO1dhV0x1WLm9cmqKvNmmcMA4uY9WlcV1dr37V7IQcdK7P-H5_HpPb5eXPi-v65sfV6uLbTe0FU6J2XRtaY5SUxkvjGKcqtAgcWNAdbxBCK0VpIAMEzwzzDoJWGLRujVQM-DH5vMstLX5vMU92HbPHvncDjttslQFeKPzfCIJzAYIVY7Mz-jTmnLCzmxTXLj1aoHYmamdcdsZltbFPRK0oax_3-dt2jeF5aY-w6J_2usve9V1yg4_5Jds0jAJVxbfc-f7EHh9f9bZdXn5nszDPtXmazoXOd0FY8D9ETDb7iIPHEBP6yYYx_vtHfwHHyKKc</recordid><startdate>19890814</startdate><enddate>19890814</enddate><creator>Richards, Anthony D.</creator><creator>Broadhurst, Anne V.</creator><creator>Ritchie, Alison J.</creator><creator>Dunn, Ben M.</creator><creator>Kay, John</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19890814</creationdate><title>Inhibition of the aspartic proteinase from HIV-2</title><author>Richards, Anthony D. ; Broadhurst, Anne V. ; Ritchie, Alison J. ; Dunn, Ben M. ; Kay, John</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5275-afbdb997669c69a2307dbe1312d8f34e1db650326d1dc292ca1d87ed88b967213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Acetyl-pepstatin</topic><topic>AIDS/HIV</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Aspartic Acid Endopeptidases</topic><topic>Biological and medical sciences</topic><topic>Endopeptidases</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. 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Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>2668032</pmid><doi>10.1016/0014-5793(89)80961-5</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1989-08, Vol.253 (1), p.214-216 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79130161 |
| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetyl-pepstatin AIDS/HIV Analytical, structural and metabolic biochemistry Aspartic Acid Endopeptidases Biological and medical sciences Endopeptidases Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology HIV, human immunodeficiency virus HIV-1 proteinase HIV-2 - enzymology HIV-2 proteinase Hydrogen-Ion Concentration Hydrolases Iva, isovaleryl Kinetics Molecular Weight Protease Inhibitors - pharmacology Renin inhibitor, H-261 Sta, 4-amino-3-hydroxy-6-methylheptanoic acid Substrate Specificity the in the sequence containing PhePro indicates the scissile peptide bond in the substrate Tight binding inhibitor |
| title | Inhibition of the aspartic proteinase from HIV-2 |
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