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Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates
Isothermal titration calorimetry (ITC) has been applied to the determination of the activity of d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/ti...
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| Published in: | Journal of biochemical and biophysical methods 2006-04, Vol.67 (1), p.57-66 |
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| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c420t-641b20509aaece8d01344506cb3f285d3fbb6b27a150c34ea69a80eac3c907b53 |
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| cites | cdi_FETCH-LOGICAL-c420t-641b20509aaece8d01344506cb3f285d3fbb6b27a150c34ea69a80eac3c907b53 |
| container_end_page | 66 |
| container_issue | 1 |
| container_start_page | 57 |
| container_title | Journal of biochemical and biophysical methods |
| container_volume | 67 |
| creator | Andújar-Sánchez, Montserrat Las Heras-Vázquez, Francisco Javier Clemente-Jiménez, Josefa María Martínez-Rodríguez, Sergio Camara-Artigas, Ana Rodríguez-Vico, Felipe Jara-Pérez, Vicente |
| description | Isothermal titration calorimetry (ITC) has been applied to the determination of the activity of
d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/time) generated. Microcalorimetric assays carried out at different temperatures provided the dependence of the catalytic rate constant on temperature. We show that ITC assay is a nondestructive method that allows the determination of the catalytic rate constant (
k
cat), Michaelis constant (
K
M), activation energy and activation Gibbs energy, enthalpy and entropy of this reaction. |
| doi_str_mv | 10.1016/j.jbbm.2006.01.002 |
| format | article |
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d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/time) generated. Microcalorimetric assays carried out at different temperatures provided the dependence of the catalytic rate constant on temperature. We show that ITC assay is a nondestructive method that allows the determination of the catalytic rate constant (
k
cat), Michaelis constant (
K
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d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/time) generated. Microcalorimetric assays carried out at different temperatures provided the dependence of the catalytic rate constant on temperature. We show that ITC assay is a nondestructive method that allows the determination of the catalytic rate constant (
k
cat), Michaelis constant (
K
M), activation energy and activation Gibbs energy, enthalpy and entropy of this reaction.</description><subject>Activation parameters</subject><subject>Activity assay</subject><subject>Amidohydrolases - chemistry</subject><subject>Calorimetry</subject><subject>d-hydantoinase</subject><subject>Hydrolysis</subject><subject>Isothermal titration calorimetry</subject><subject>Kinetics</subject><subject>Recombinant Proteins - chemistry</subject><subject>Rhizobium - enzymology</subject><subject>Substrate Specificity</subject><subject>Thermodynamics</subject><issn>0165-022X</issn><issn>1872-857X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNp9kc1u1DAUhSMEokPhBVggr9glXDu_I7FBpVCkSmxA6s66dm5Uj5J48PWMlL4Vb4gzM4gdqyzu952j-GTZWwmFBNl82BU7Y6ZCATQFyAJAPcs2smtV3tXtw_Nsk6A6B6UerrJXzDsAKDtVvcyuZFNt27IrN9nv2_lpmTA6K9BGd3RxEciMi_CD6PPHpcc5ejcjkzCLcOzjI4UJRxFdDMnzs7A4-uAmimEpxGeK6Z6E0ymFJF6cHN8vM05_i873PQacVoPF4MOJTZXBjws7Xm2mI4XUxgfDax_x6-zFgCPTm8v3Ovv55fbHzV1-__3rt5tP97mtFMS8qaRRUMMWkSx1PciyqmporCkH1dV9ORjTGNWirMGWFWGzxQ4IbWm30Jq6vM7en3P3wf86EEc9ObY0jjiTP7Bu2raVndomUJ1BGzxzoEHv02tgWLQEvQ6ld3odSq9DaZA6DZWkd5f0g5mo_6dclknAxzNA6R-PjoJm62i21LtANureu__l_wEMIqsB</recordid><startdate>20060430</startdate><enddate>20060430</enddate><creator>Andújar-Sánchez, Montserrat</creator><creator>Las Heras-Vázquez, Francisco Javier</creator><creator>Clemente-Jiménez, Josefa María</creator><creator>Martínez-Rodríguez, Sergio</creator><creator>Camara-Artigas, Ana</creator><creator>Rodríguez-Vico, Felipe</creator><creator>Jara-Pérez, Vicente</creator><general>Elsevier B.V</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>20060430</creationdate><title>Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates</title><author>Andújar-Sánchez, Montserrat ; Las Heras-Vázquez, Francisco Javier ; Clemente-Jiménez, Josefa María ; Martínez-Rodríguez, Sergio ; Camara-Artigas, Ana ; Rodríguez-Vico, Felipe ; Jara-Pérez, Vicente</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-641b20509aaece8d01344506cb3f285d3fbb6b27a150c34ea69a80eac3c907b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Activation parameters</topic><topic>Activity assay</topic><topic>Amidohydrolases - chemistry</topic><topic>Calorimetry</topic><topic>d-hydantoinase</topic><topic>Hydrolysis</topic><topic>Isothermal titration calorimetry</topic><topic>Kinetics</topic><topic>Recombinant Proteins - chemistry</topic><topic>Rhizobium - enzymology</topic><topic>Substrate Specificity</topic><topic>Thermodynamics</topic><toplevel>online_resources</toplevel><creatorcontrib>Andújar-Sánchez, Montserrat</creatorcontrib><creatorcontrib>Las Heras-Vázquez, Francisco Javier</creatorcontrib><creatorcontrib>Clemente-Jiménez, Josefa María</creatorcontrib><creatorcontrib>Martínez-Rodríguez, Sergio</creatorcontrib><creatorcontrib>Camara-Artigas, Ana</creatorcontrib><creatorcontrib>Rodríguez-Vico, Felipe</creatorcontrib><creatorcontrib>Jara-Pérez, Vicente</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>Journal of biochemical and biophysical methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Andújar-Sánchez, Montserrat</au><au>Las Heras-Vázquez, Francisco Javier</au><au>Clemente-Jiménez, Josefa María</au><au>Martínez-Rodríguez, Sergio</au><au>Camara-Artigas, Ana</au><au>Rodríguez-Vico, Felipe</au><au>Jara-Pérez, Vicente</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates</atitle><jtitle>Journal of biochemical and biophysical methods</jtitle><addtitle>J Biochem Biophys Methods</addtitle><date>2006-04-30</date><risdate>2006</risdate><volume>67</volume><issue>1</issue><spage>57</spage><epage>66</epage><pages>57-66</pages><issn>0165-022X</issn><eissn>1872-857X</eissn><abstract>Isothermal titration calorimetry (ITC) has been applied to the determination of the activity of
d-hydantoinase (EC 3.5.2.2) with several substrates by monitoring the heat released during the reaction. The method is based on the proportionality between the reaction rate and the thermal power (heat/time) generated. Microcalorimetric assays carried out at different temperatures provided the dependence of the catalytic rate constant on temperature. We show that ITC assay is a nondestructive method that allows the determination of the catalytic rate constant (
k
cat), Michaelis constant (
K
M), activation energy and activation Gibbs energy, enthalpy and entropy of this reaction.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>16497383</pmid><doi>10.1016/j.jbbm.2006.01.002</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of biochemical and biophysical methods, 2006-04, Vol.67 (1), p.57-66 |
| issn | 0165-022X 1872-857X |
| language | eng |
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| source | Elsevier |
| subjects | Activation parameters Activity assay Amidohydrolases - chemistry Calorimetry d-hydantoinase Hydrolysis Isothermal titration calorimetry Kinetics Recombinant Proteins - chemistry Rhizobium - enzymology Substrate Specificity Thermodynamics |
| title | Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates |
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