Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride
Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2014, Vol.172 (2), p.854-866 |
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| creator | Barreca, D Lagan , G Ficarra, S Tellone, E Leuzzi, U Galtieri, A Bellocco, E |
| description | Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea. |
| doi_str_mv | 10.1007/s12010-013-0580-9 |
| format | Article |
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Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-013-0580-9</identifier><identifier>PMID: 24122710</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>additives ; Animals ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Circular Dichroism ; Electrophoresis, Agar Gel ; Enzyme Activation - drug effects ; Enzymes ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Guanidine - pharmacology ; High temperature ; hydrophobicity ; Kinetics ; ornithine carbamoyltransferase ; Ornithine Carbamoyltransferase - metabolism ; Protein Folding - drug effects ; Protein Structure, Secondary ; Sharks ; Spectrophotometry, Ultraviolet ; Spectrum analysis ; temperature ; Thermodynamics ; ultraviolet-visible spectroscopy ; Urea ; Urea - pharmacology</subject><ispartof>Applied biochemistry and biotechnology, 2014, Vol.172 (2), p.854-866</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media New York 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-113606c84022fd128a02c7dc26b96e1b32696b20b5c59bc559e3f49cd3a4bdd63</citedby><cites>FETCH-LOGICAL-c459t-113606c84022fd128a02c7dc26b96e1b32696b20b5c59bc559e3f49cd3a4bdd63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-013-0580-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-013-0580-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,4024,27923,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28562445$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24122710$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barreca, D</creatorcontrib><creatorcontrib>Lagan , G</creatorcontrib><creatorcontrib>Ficarra, S</creatorcontrib><creatorcontrib>Tellone, E</creatorcontrib><creatorcontrib>Leuzzi, U</creatorcontrib><creatorcontrib>Galtieri, A</creatorcontrib><creatorcontrib>Bellocco, E</creatorcontrib><title>Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.</description><subject>additives</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Circular Dichroism</subject><subject>Electrophoresis, Agar Gel</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanidine - pharmacology</subject><subject>High temperature</subject><subject>hydrophobicity</subject><subject>Kinetics</subject><subject>ornithine carbamoyltransferase</subject><subject>Ornithine Carbamoyltransferase - metabolism</subject><subject>Protein Folding - drug effects</subject><subject>Protein Structure, Secondary</subject><subject>Sharks</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectrum analysis</subject><subject>temperature</subject><subject>Thermodynamics</subject><subject>ultraviolet-visible spectroscopy</subject><subject>Urea</subject><subject>Urea - pharmacology</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU2LFDEQhoMo7rj6A7xoQAQvrZXqTqdzlEF3hYUV1jmHdFI900tPsibdh_n3ZpjxAw_iKYc89Va9PIy9FPBeAKgPWSAIqEDUFcgOKv2IrYSUugLU4jFbAaq6Quz0BXuW8z2AwE6qp-wCG4GoBKyYu01hnHdjIL62qbf7eJjmZEMeKNlMfBOGOPkxbPndbGfKfAx83hH_mihTcMTjwDeJLLfB86vFhtEfs64PPkW3m2IaPT1nTwY7ZXpxfi_Z5vOnb-vr6ub26sv6403lGqnnSoi6hdZ1DSAOvpxqAZ3yDttetyT6Glvd9gi9dFL3rvSkemi087Vteu_b-pK9O-U-pPh9oTyb_ZgdTZMNFJdshBRQwpsG_wMFWWOndFfQN3-h93FJoRQxQilosFV43C1OlEsx50SDeUjj3qaDEWCOssxJlimyzFGW0WXm1Tl56ffkf038tFOAt2fAZmenoXhxY_7NdbItbWTh8MTl8hW2lP448R_bX5-GBhuN3aYSvLkrUAMAEpWS9Q8eZLPJ</recordid><startdate>2014</startdate><enddate>2014</enddate><creator>Barreca, D</creator><creator>Lagan , G</creator><creator>Ficarra, S</creator><creator>Tellone, E</creator><creator>Leuzzi, U</creator><creator>Galtieri, A</creator><creator>Bellocco, E</creator><general>Springer-Verlag</general><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>2014</creationdate><title>Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride</title><author>Barreca, D ; Lagan , G ; Ficarra, S ; Tellone, E ; Leuzzi, U ; Galtieri, A ; Bellocco, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-113606c84022fd128a02c7dc26b96e1b32696b20b5c59bc559e3f49cd3a4bdd63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>additives</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Circular Dichroism</topic><topic>Electrophoresis, Agar Gel</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Fundamental and applied biological sciences. 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Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><pmid>24122710</pmid><doi>10.1007/s12010-013-0580-9</doi><tpages>13</tpages></addata></record> |
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| subjects | additives Animals Biochemistry Biological and medical sciences Biotechnology Chemistry Chemistry and Materials Science Circular Dichroism Electrophoresis, Agar Gel Enzyme Activation - drug effects Enzymes Fluorescence Fundamental and applied biological sciences. Psychology Guanidine - pharmacology High temperature hydrophobicity Kinetics ornithine carbamoyltransferase Ornithine Carbamoyltransferase - metabolism Protein Folding - drug effects Protein Structure, Secondary Sharks Spectrophotometry, Ultraviolet Spectrum analysis temperature Thermodynamics ultraviolet-visible spectroscopy Urea Urea - pharmacology |
| title | Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride |
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