Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius
The Arabian camel, Camelus dromedarius is naturally adapted to extreme desert climate and has evolved protective mechanisms to limit oxidative stress. The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellula...
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| Veröffentlicht in: | International journal of biological macromolecules 2016-07, Vol.88, p.313-319 |
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| creator | Malik, Ajamaluddin Fouad, Dalia Labrou, Nikolaos E. Al-Senaidy, Abdulrahman M. Ismael, Mohamed A. Saeed, Hesham M. Ataya, Farid S. |
| description | The Arabian camel, Camelus dromedarius is naturally adapted to extreme desert climate and has evolved protective mechanisms to limit oxidative stress. The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellular Phase II detoxification machinery and is involved in the protection against oxidative stress and xenobiotics. In the present study, C. dromedarius kappa class glutathione transferase (CdGSTK1-1) was cloned, expressed in E. coli BL21, purified and its structural, thermodynamic and unfolding pathway was investigated. The results showed that CdGSTK1-1 has unique trimeric structure, exhibits low thermostability and a complex equilibrium unfolding profile. It unfolds through three folding states with formation of thinly populated intermediate species. The melting points (Tm) of the first unfolding transition was 40.3±0.2°C and Tm of the second unfolding transition was 49.1±0.1°C. The van’t Hoff enthalpy of the first and second transition were 298.7±13.2 and 616.5±2.4kJ/mol, respectively. Moreover, intrinsic fluorescence and near-UV CD studies indicates that substrate binding does not leads to major conformational changes in CdGSTK1-1. |
| doi_str_mv | 10.1016/j.ijbiomac.2016.03.065 |
| format | Article |
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The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellular Phase II detoxification machinery and is involved in the protection against oxidative stress and xenobiotics. In the present study, C. dromedarius kappa class glutathione transferase (CdGSTK1-1) was cloned, expressed in E. coli BL21, purified and its structural, thermodynamic and unfolding pathway was investigated. The results showed that CdGSTK1-1 has unique trimeric structure, exhibits low thermostability and a complex equilibrium unfolding profile. It unfolds through three folding states with formation of thinly populated intermediate species. The melting points (Tm) of the first unfolding transition was 40.3±0.2°C and Tm of the second unfolding transition was 49.1±0.1°C. The van’t Hoff enthalpy of the first and second transition were 298.7±13.2 and 616.5±2.4kJ/mol, respectively. Moreover, intrinsic fluorescence and near-UV CD studies indicates that substrate binding does not leads to major conformational changes in CdGSTK1-1.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2016.03.065</identifier><identifier>PMID: 27044344</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Adaptation, Physiological ; Animals ; Camelus - metabolism ; Camelus dromedarius ; Cloning, Molecular ; Desert Climate ; Dynamic multimode spectroscopy ; Enzyme Stability ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Folding ; Gene Expression ; Glutathione Transferase - chemistry ; Glutathione Transferase - genetics ; Hot Temperature ; Isoenzymes - chemistry ; Isoenzymes - genetics ; Kappa class GST ; Protein Folding ; Protein stability ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Unfolding ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Thermodynamics</subject><ispartof>International journal of biological macromolecules, 2016-07, Vol.88, p.313-319</ispartof><rights>2016 Elsevier B.V.</rights><rights>Copyright © 2016 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-2dbd64d4ec5385191ac6efffb763e7b2d3ffc430d23e8334c27e19a66279c2db3</citedby><cites>FETCH-LOGICAL-c368t-2dbd64d4ec5385191ac6efffb763e7b2d3ffc430d23e8334c27e19a66279c2db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2016.03.065$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27044344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malik, Ajamaluddin</creatorcontrib><creatorcontrib>Fouad, Dalia</creatorcontrib><creatorcontrib>Labrou, Nikolaos E.</creatorcontrib><creatorcontrib>Al-Senaidy, Abdulrahman M.</creatorcontrib><creatorcontrib>Ismael, Mohamed A.</creatorcontrib><creatorcontrib>Saeed, Hesham M.</creatorcontrib><creatorcontrib>Ataya, Farid S.</creatorcontrib><title>Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>The Arabian camel, Camelus dromedarius is naturally adapted to extreme desert climate and has evolved protective mechanisms to limit oxidative stress. The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellular Phase II detoxification machinery and is involved in the protection against oxidative stress and xenobiotics. In the present study, C. dromedarius kappa class glutathione transferase (CdGSTK1-1) was cloned, expressed in E. coli BL21, purified and its structural, thermodynamic and unfolding pathway was investigated. The results showed that CdGSTK1-1 has unique trimeric structure, exhibits low thermostability and a complex equilibrium unfolding profile. It unfolds through three folding states with formation of thinly populated intermediate species. The melting points (Tm) of the first unfolding transition was 40.3±0.2°C and Tm of the second unfolding transition was 49.1±0.1°C. The van’t Hoff enthalpy of the first and second transition were 298.7±13.2 and 616.5±2.4kJ/mol, respectively. Moreover, intrinsic fluorescence and near-UV CD studies indicates that substrate binding does not leads to major conformational changes in CdGSTK1-1.</description><subject>Adaptation, Physiological</subject><subject>Animals</subject><subject>Camelus - metabolism</subject><subject>Camelus dromedarius</subject><subject>Cloning, Molecular</subject><subject>Desert Climate</subject><subject>Dynamic multimode spectroscopy</subject><subject>Enzyme Stability</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Folding</subject><subject>Gene Expression</subject><subject>Glutathione Transferase - chemistry</subject><subject>Glutathione Transferase - genetics</subject><subject>Hot Temperature</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Kappa class GST</subject><subject>Protein Folding</subject><subject>Protein stability</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Unfolding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Thermodynamics</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtv1TAQhS0EoreFv1B5ySapHTt2sgNd8ZIqsQDW1sQet74kcbAdpP57XN2WLavRGZ0zj4-Qa85azri6ObXhNIW4gG27qlsmWqb6F-TABz02jDHxkhwYl7wZuGAX5DLnU-2qng-vyUWnmZRCygO5-17SbsueYKawOlruMS3RPaywBEu3FDdMJWCm0dNfsG1A7Qw507t5L1DuQ1yRlgRr9pggI_UpLvQIC857pq4KdJDCnt-QVx7mjG-f6hX5-enjj-OX5vbb56_HD7eNFWooTecmp6STaHsx9HzkYBV67yetBOqpc8J7KwVzncBBCGk7jXwEpTo92hoWV-TdeW49_feOuZglZIvzDCvGPRuuh1Er1mtRrepstSnmnNCbLYUF0oPhzDxCNifzDNk8QjZMmEqwBq-fduxT_e9f7JlqNbw_G7B--idgMtkGXC26kNAW42L4346_DE-UCw</recordid><startdate>201607</startdate><enddate>201607</enddate><creator>Malik, Ajamaluddin</creator><creator>Fouad, Dalia</creator><creator>Labrou, Nikolaos E.</creator><creator>Al-Senaidy, Abdulrahman M.</creator><creator>Ismael, Mohamed A.</creator><creator>Saeed, Hesham M.</creator><creator>Ataya, Farid S.</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>201607</creationdate><title>Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius</title><author>Malik, Ajamaluddin ; 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The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellular Phase II detoxification machinery and is involved in the protection against oxidative stress and xenobiotics. In the present study, C. dromedarius kappa class glutathione transferase (CdGSTK1-1) was cloned, expressed in E. coli BL21, purified and its structural, thermodynamic and unfolding pathway was investigated. The results showed that CdGSTK1-1 has unique trimeric structure, exhibits low thermostability and a complex equilibrium unfolding profile. It unfolds through three folding states with formation of thinly populated intermediate species. The melting points (Tm) of the first unfolding transition was 40.3±0.2°C and Tm of the second unfolding transition was 49.1±0.1°C. The van’t Hoff enthalpy of the first and second transition were 298.7±13.2 and 616.5±2.4kJ/mol, respectively. 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| subjects | Adaptation, Physiological Animals Camelus - metabolism Camelus dromedarius Cloning, Molecular Desert Climate Dynamic multimode spectroscopy Enzyme Stability Escherichia coli - genetics Escherichia coli - metabolism Folding Gene Expression Glutathione Transferase - chemistry Glutathione Transferase - genetics Hot Temperature Isoenzymes - chemistry Isoenzymes - genetics Kappa class GST Protein Folding Protein stability Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Protein Unfolding Recombinant Proteins - chemistry Recombinant Proteins - genetics Thermodynamics |
| title | Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius |
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