Conformational stabilization of enzymes in covalent catalysis
The enzymes aspartate aminotransferase, rhodanese, and chymotrypsin form covalent substituted-enzyme intermediates during the course of their catalysis. The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to in...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1978-04, Vol.187 (1), p.163-169 |
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| container_end_page | 169 |
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| container_issue | 1 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 187 |
| creator | Volini, Marguerite Wang, Shu-Fang |
| description | The enzymes aspartate aminotransferase, rhodanese, and chymotrypsin form covalent substituted-enzyme intermediates during the course of their catalysis. The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to inert forms that occur in the free enzyme species and other forms not covalently substituted. |
| doi_str_mv | 10.1016/0003-9861(78)90019-X |
| format | Article |
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The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to inert forms that occur in the free enzyme species and other forms not covalently substituted.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(78)90019-X</identifier><identifier>PMID: 26312</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aspartate Aminotransferases - metabolism ; Catalysis ; Chemical Phenomena ; Chemistry ; Chymotrypsin - metabolism ; Circular Dichroism ; Hydrogen-Ion Concentration ; Optical Rotatory Dispersion ; Protein Conformation ; Sulfurtransferases - metabolism ; Thiosulfate Sulfurtransferase - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1978-04, Vol.187 (1), p.163-169</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c355t-2d74ff91c6b6a6e7c7b7be8890338cbdf015a4f77ee415821b531d6bd2e0a99e3</citedby><cites>FETCH-LOGICAL-c355t-2d74ff91c6b6a6e7c7b7be8890338cbdf015a4f77ee415821b531d6bd2e0a99e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/000398617890019X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26312$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Volini, Marguerite</creatorcontrib><creatorcontrib>Wang, Shu-Fang</creatorcontrib><title>Conformational stabilization of enzymes in covalent catalysis</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The enzymes aspartate aminotransferase, rhodanese, and chymotrypsin form covalent substituted-enzyme intermediates during the course of their catalysis. The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to inert forms that occur in the free enzyme species and other forms not covalently substituted.</description><subject>Aspartate Aminotransferases - metabolism</subject><subject>Catalysis</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chymotrypsin - metabolism</subject><subject>Circular Dichroism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Optical Rotatory Dispersion</subject><subject>Protein Conformation</subject><subject>Sulfurtransferases - metabolism</subject><subject>Thiosulfate Sulfurtransferase - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoNYtFZ_gR72JHpYTTbZZHNQkOIXFLwo9BaS7AQiuxtNtoX217v9oEdPwzDP-8I8CF0RfEcw4fcYY5rLipMbUd1KjInM50doTLDkOaYVO0bjA3KKzlL6HhjCeHGCRgWnpBijh2noXIit7n3odJOlXhvf-PV2z4LLoFuvWkiZ7zIblrqBrs-s7nWzSj6do5HTTYKL_Zygr5fnz-lbPvt4fZ8-zXJLy7LPi1ow5ySx3HDNQVhhhIGqkpjSypraYVJq5oQAYKSsCmJKSmpu6gKwlhLoBF3ven9i-F1A6lXrk4Wm0R2ERVKCYcp4WQ4g24E2hpQiOPUTfavjShGsNs7URojaCFGiUltnaj7ELvf9C9NCfQhtJQ3Xx90VhheXHqJK1kNnofYRbK_q4P-v_wMEgnvI</recordid><startdate>19780415</startdate><enddate>19780415</enddate><creator>Volini, Marguerite</creator><creator>Wang, Shu-Fang</creator><general>Elsevier Inc</general><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>19780415</creationdate><title>Conformational stabilization of enzymes in covalent catalysis</title><author>Volini, Marguerite ; Wang, Shu-Fang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-2d74ff91c6b6a6e7c7b7be8890338cbdf015a4f77ee415821b531d6bd2e0a99e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Aspartate Aminotransferases - metabolism</topic><topic>Catalysis</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chymotrypsin - metabolism</topic><topic>Circular Dichroism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Optical Rotatory Dispersion</topic><topic>Protein Conformation</topic><topic>Sulfurtransferases - metabolism</topic><topic>Thiosulfate Sulfurtransferase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Volini, Marguerite</creatorcontrib><creatorcontrib>Wang, Shu-Fang</creatorcontrib><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Volini, Marguerite</au><au>Wang, Shu-Fang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational stabilization of enzymes in covalent catalysis</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1978-04-15</date><risdate>1978</risdate><volume>187</volume><issue>1</issue><spage>163</spage><epage>169</epage><pages>163-169</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The enzymes aspartate aminotransferase, rhodanese, and chymotrypsin form covalent substituted-enzyme intermediates during the course of their catalysis. The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to inert forms that occur in the free enzyme species and other forms not covalently substituted.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>26312</pmid><doi>10.1016/0003-9861(78)90019-X</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1978-04, Vol.187 (1), p.163-169 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74034655 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Aspartate Aminotransferases - metabolism Catalysis Chemical Phenomena Chemistry Chymotrypsin - metabolism Circular Dichroism Hydrogen-Ion Concentration Optical Rotatory Dispersion Protein Conformation Sulfurtransferases - metabolism Thiosulfate Sulfurtransferase - metabolism |
| title | Conformational stabilization of enzymes in covalent catalysis |
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