Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach
Abstract Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2017-03, Vol.30 (3), p.219-226 |
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| creator | Van Elzen, R. Schoenmakers, E. Brandt, I. Van Der Veken, P. Lambeir, A.M. |
| description | Abstract
Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to find a suitable method to study enzyme kinetics with an unmodified biological substrate. It was found that human PREP behaves identically to the porcine homolog, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV). However, the empirical temperature coefficient Q10, describing the temperature dependency of the kinetic parameters and the non-linear Arrhenius plot of kcat/Km are common characteristics between PREP and DPP IV. The results also demonstrate the feasibility of microcalorimetry for measuring turn-over of proline containing peptides. |
| doi_str_mv | 10.1093/protein/gzw079 |
| format | Article |
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Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to find a suitable method to study enzyme kinetics with an unmodified biological substrate. It was found that human PREP behaves identically to the porcine homolog, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV). However, the empirical temperature coefficient Q10, describing the temperature dependency of the kinetic parameters and the non-linear Arrhenius plot of kcat/Km are common characteristics between PREP and DPP IV. The results also demonstrate the feasibility of microcalorimetry for measuring turn-over of proline containing peptides.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzw079</identifier><identifier>PMID: 28062644</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Enzyme Stability ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Mitochondrial Proteins - chemistry ; Mitochondrial Proteins - metabolism ; Protein Domains ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - metabolism ; Swine</subject><ispartof>Protein engineering, design and selection, 2017-03, Vol.30 (3), p.219-226</ispartof><rights>The Author 2017. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2017</rights><rights>The Author 2017. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369t-c0a322b0f6170bba43ac8c1538377897917b1505502fa25350027c1392b7f2b3</citedby><cites>FETCH-LOGICAL-c369t-c0a322b0f6170bba43ac8c1538377897917b1505502fa25350027c1392b7f2b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28062644$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Elzen, R.</creatorcontrib><creatorcontrib>Schoenmakers, E.</creatorcontrib><creatorcontrib>Brandt, I.</creatorcontrib><creatorcontrib>Van Der Veken, P.</creatorcontrib><creatorcontrib>Lambeir, A.M.</creatorcontrib><title>Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach</title><title>Protein engineering, design and selection</title><addtitle>Protein Eng Des Sel</addtitle><description>Abstract
Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to find a suitable method to study enzyme kinetics with an unmodified biological substrate. It was found that human PREP behaves identically to the porcine homolog, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV). However, the empirical temperature coefficient Q10, describing the temperature dependency of the kinetic parameters and the non-linear Arrhenius plot of kcat/Km are common characteristics between PREP and DPP IV. The results also demonstrate the feasibility of microcalorimetry for measuring turn-over of proline containing peptides.</description><subject>Animals</subject><subject>Enzyme Stability</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Mitochondrial Proteins - chemistry</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Protein Domains</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Swine</subject><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EoqWwMiKPMKT1R2wnbKjiS6qEhLpHF8dJDYkd4kSo_HqCUliZ7obn3vf0IHRJyZKSlK_azvfGulX19UlUeoTmVMU0IpTHx387kzN0FsIbIUwqSk_RjCVEMhnHc_S6sRW4IrKuGLQpsPau9F0DvfUOaqx34CoTsHV4bKr3Nfa1rXxr2t4WEMwtBvxunemtxtCOCOjdOTopoQ7m4jAXaPtwv10_RZuXx-f13SbSXKZ9pAlwxnJSSqpInkPMQSeaCp5wpZJUpVTlVBAhCCuBCS7G95WmPGW5KlnOF-h6ih1bPwYT-qyxQZu6Bmf8EDKaCClSRaQY0eWE6s6H0JkyazvbQLfPKMl-NGYHjdmkcTy4OmQPeWOKP_zX2wjcTIAf2v_CvgE3LH7S</recordid><startdate>20170301</startdate><enddate>20170301</enddate><creator>Van Elzen, R.</creator><creator>Schoenmakers, E.</creator><creator>Brandt, I.</creator><creator>Van Der Veken, P.</creator><creator>Lambeir, A.M.</creator><general>Oxford University Press</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>20170301</creationdate><title>Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach</title><author>Van Elzen, R. ; Schoenmakers, E. ; Brandt, I. ; Van Der Veken, P. ; Lambeir, A.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-c0a322b0f6170bba43ac8c1538377897917b1505502fa25350027c1392b7f2b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Enzyme Stability</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Mitochondrial Proteins - chemistry</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Protein Domains</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Elzen, R.</creatorcontrib><creatorcontrib>Schoenmakers, E.</creatorcontrib><creatorcontrib>Brandt, I.</creatorcontrib><creatorcontrib>Van Der Veken, P.</creatorcontrib><creatorcontrib>Lambeir, A.M.</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>Protein engineering, design and selection</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Elzen, R.</au><au>Schoenmakers, E.</au><au>Brandt, I.</au><au>Van Der Veken, P.</au><au>Lambeir, A.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach</atitle><jtitle>Protein engineering, design and selection</jtitle><addtitle>Protein Eng Des Sel</addtitle><date>2017-03-01</date><risdate>2017</risdate><volume>30</volume><issue>3</issue><spage>219</spage><epage>226</epage><pages>219-226</pages><issn>1741-0126</issn><eissn>1741-0134</eissn><abstract>Abstract
Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to find a suitable method to study enzyme kinetics with an unmodified biological substrate. It was found that human PREP behaves identically to the porcine homolog, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV). However, the empirical temperature coefficient Q10, describing the temperature dependency of the kinetic parameters and the non-linear Arrhenius plot of kcat/Km are common characteristics between PREP and DPP IV. The results also demonstrate the feasibility of microcalorimetry for measuring turn-over of proline containing peptides.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>28062644</pmid><doi>10.1093/protein/gzw079</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Enzyme Stability Humans Hydrogen-Ion Concentration Kinetics Mitochondrial Proteins - chemistry Mitochondrial Proteins - metabolism Protein Domains Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Swine |
| title | Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach |
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