Transient model of thermal deactivation of enzymes
The kinetics of enzyme deactivation provide useful insights on processes that determine the level of biological function of any enzyme. Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused...
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| Veröffentlicht in: | Biochimica et biophysica acta 2011-10, Vol.1814 (10), p.1318-1324 |
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| container_title | Biochimica et biophysica acta |
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| creator | Chen, Nelson G. Gregory, Kalvin Sun, Ye Golovlev, Val |
| description | The kinetics of enzyme deactivation provide useful insights on processes that determine the level of biological function of any enzyme.
Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.
►Enzyme deactivation upon heating proceeds in multiple steps ►Deactivation is rapid, when compared to denaturation ►Transient model to describe sequential changes — different from Equilibrium model |
| doi_str_mv | 10.1016/j.bbapap.2011.06.010 |
| format | Article |
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Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.
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Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.
►Enzyme deactivation upon heating proceeds in multiple steps ►Deactivation is rapid, when compared to denaturation ►Transient model to describe sequential changes — different from Equilibrium model</description><subject>Animals</subject><subject>Deactivation</subject><subject>Denaturation</subject><subject>Enzyme</subject><subject>Enzyme Activation</subject><subject>enzyme inactivation</subject><subject>enzyme kinetics</subject><subject>Enzyme Stability - physiology</subject><subject>Fireflies - enzymology</subject><subject>Fireflies - metabolism</subject><subject>Heating</subject><subject>Kinetics</subject><subject>luciferase</subject><subject>Luciferases, Firefly - chemistry</subject><subject>Luciferases, Firefly - metabolism</subject><subject>Models, Biological</subject><subject>Photinus pyralis</subject><subject>Protein</subject><subject>Protein Denaturation</subject><subject>Temperature</subject><subject>Time Factors</subject><issn>1570-9639</issn><issn>0006-3002</issn><issn>1878-1454</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1vFDEMhiMEoqXlHyDYI5cZ8jXJ5IKEKihIlXpoe7aSjNNmNTNZktmVyq8n2y0FLj3Fiu3Xrx8T8o7RllGmPq1b5-zGblpOGWupaimjL8gx63XfMNnJlzXuNG2MEuaIvCllTSmnWnevyRFnWhojumPCr7OdS8R5WU1pwHGVwmq5wzzZcTWg9Uvc2SWmef-P86_7CcspeRXsWPDt43tCbr59vT773lxcnv84-3LReNnrpZHCmM5hdaIFMmGlVkx3wTsMKtQNnA9cS_Sh5oTkUpnglbOWCdM7J6U4IZ8Puputm3Dw1WO2I2xynGy-h2Qj_J-Z4x3cph0IpjntRRX4-CiQ088tlgWmWDyOo50xbQuwngsjO_UwSx5KfU6lZAxPYxiFPW5YwwE37HEDVVBx17b3_1p8avrDtxZ8OBQEm8De5ljg5qoqdPUWTEpu_m6JFeUuYobi6zk8DjGjX2BI8XkPvwHdrJxP</recordid><startdate>20111001</startdate><enddate>20111001</enddate><creator>Chen, Nelson G.</creator><creator>Gregory, Kalvin</creator><creator>Sun, Ye</creator><creator>Golovlev, Val</creator><general>Elsevier B.V</general><scope>FBQ</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>20111001</creationdate><title>Transient model of thermal deactivation of enzymes</title><author>Chen, Nelson G. ; Gregory, Kalvin ; Sun, Ye ; Golovlev, Val</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-43995be45473e13a476175fcbef6f101bcf274ecf13a342469fc6baa1398bb443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Deactivation</topic><topic>Denaturation</topic><topic>Enzyme</topic><topic>Enzyme Activation</topic><topic>enzyme inactivation</topic><topic>enzyme kinetics</topic><topic>Enzyme Stability - physiology</topic><topic>Fireflies - enzymology</topic><topic>Fireflies - metabolism</topic><topic>Heating</topic><topic>Kinetics</topic><topic>luciferase</topic><topic>Luciferases, Firefly - chemistry</topic><topic>Luciferases, Firefly - metabolism</topic><topic>Models, Biological</topic><topic>Photinus pyralis</topic><topic>Protein</topic><topic>Protein Denaturation</topic><topic>Temperature</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Nelson G.</creatorcontrib><creatorcontrib>Gregory, Kalvin</creatorcontrib><creatorcontrib>Sun, Ye</creatorcontrib><creatorcontrib>Golovlev, Val</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Nelson G.</au><au>Gregory, Kalvin</au><au>Sun, Ye</au><au>Golovlev, Val</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transient model of thermal deactivation of enzymes</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2011-10-01</date><risdate>2011</risdate><volume>1814</volume><issue>10</issue><spage>1318</spage><epage>1324</epage><pages>1318-1324</pages><issn>1570-9639</issn><issn>0006-3002</issn><eissn>1878-1454</eissn><abstract>The kinetics of enzyme deactivation provide useful insights on processes that determine the level of biological function of any enzyme.
Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.
►Enzyme deactivation upon heating proceeds in multiple steps ►Deactivation is rapid, when compared to denaturation ►Transient model to describe sequential changes — different from Equilibrium model</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>21749935</pmid><doi>10.1016/j.bbapap.2011.06.010</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Deactivation Denaturation Enzyme Enzyme Activation enzyme inactivation enzyme kinetics Enzyme Stability - physiology Fireflies - enzymology Fireflies - metabolism Heating Kinetics luciferase Luciferases, Firefly - chemistry Luciferases, Firefly - metabolism Models, Biological Photinus pyralis Protein Protein Denaturation Temperature Time Factors |
| title | Transient model of thermal deactivation of enzymes |
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