Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021
A novel oligomeric SGNH-arylesterase (Sm23) from Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser 10, Asp 187, and His 190) and oxyanion holes (Ser 10-Gly 50-A...
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| Veröffentlicht in: | International journal of biological macromolecules 2010-03, Vol.46 (2), p.145-152 |
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| container_title | International journal of biological macromolecules |
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| creator | Hwang, Heejin Kim, SeungBum Yoon, Sangyoung Ryu, Yeonwoo Lee, Sang Yoon Kim, T. Doohun |
| description | A novel oligomeric SGNH-arylesterase (Sm23) from
Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser
10, Asp
187, and His
190) and oxyanion holes (Ser
10-Gly
50-Asn
90). The wild type enzyme was able to hydrolyze
p-nitrophenyl acetate, α- and β-naphthyl acetate, while S10A mutant completely lost its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. Furthermore, spherical or globular aggregates were observed with 1-butyl-3-methylimidazolium tetrafluoroborate, while amorphous aggregates were formed with 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide. |
| doi_str_mv | 10.1016/j.ijbiomac.2009.12.010 |
| format | Article |
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Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser
10, Asp
187, and His
190) and oxyanion holes (Ser
10-Gly
50-Asn
90). The wild type enzyme was able to hydrolyze
p-nitrophenyl acetate, α- and β-naphthyl acetate, while S10A mutant completely lost its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. Furthermore, spherical or globular aggregates were observed with 1-butyl-3-methylimidazolium tetrafluoroborate, while amorphous aggregates were formed with 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2009.12.010</identifier><identifier>PMID: 20060410</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Carboxylic Ester Hydrolases - chemistry ; Carboxylic Ester Hydrolases - metabolism ; Carboxylic Ester Hydrolases - ultrastructure ; Circular Dichroism ; Electrophoresis, Polyacrylamide Gel ; Enzyme Assays ; Light ; Molecular Sequence Data ; p-Nitrophenyl acetate ; Protein Conformation ; Scattering, Radiation ; Sequence Alignment ; Sequence Analysis, Protein ; SGNH-arylesterase ; Sinorhizobium meliloti - enzymology ; Solvents ; Spectrometry, Fluorescence ; Staining and Labeling ; Stereoisomerism ; Structural analysis ; Substrate Specificity</subject><ispartof>International journal of biological macromolecules, 2010-03, Vol.46 (2), p.145-152</ispartof><rights>2010 Elsevier B.V.</rights><rights>2010 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c367t-91494dcc94b88501f31e39b825397214189a31f893c157c94ef1527de955c4173</citedby><cites>FETCH-LOGICAL-c367t-91494dcc94b88501f31e39b825397214189a31f893c157c94ef1527de955c4173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141813010000024$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20060410$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hwang, Heejin</creatorcontrib><creatorcontrib>Kim, SeungBum</creatorcontrib><creatorcontrib>Yoon, Sangyoung</creatorcontrib><creatorcontrib>Ryu, Yeonwoo</creatorcontrib><creatorcontrib>Lee, Sang Yoon</creatorcontrib><creatorcontrib>Kim, T. Doohun</creatorcontrib><title>Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>A novel oligomeric SGNH-arylesterase (Sm23) from
Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser
10, Asp
187, and His
190) and oxyanion holes (Ser
10-Gly
50-Asn
90). The wild type enzyme was able to hydrolyze
p-nitrophenyl acetate, α- and β-naphthyl acetate, while S10A mutant completely lost its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. Furthermore, spherical or globular aggregates were observed with 1-butyl-3-methylimidazolium tetrafluoroborate, while amorphous aggregates were formed with 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide.</description><subject>Amino Acid Sequence</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Carboxylic Ester Hydrolases - ultrastructure</subject><subject>Circular Dichroism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Assays</subject><subject>Light</subject><subject>Molecular Sequence Data</subject><subject>p-Nitrophenyl acetate</subject><subject>Protein Conformation</subject><subject>Scattering, Radiation</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><subject>SGNH-arylesterase</subject><subject>Sinorhizobium meliloti - enzymology</subject><subject>Solvents</subject><subject>Spectrometry, Fluorescence</subject><subject>Staining and Labeling</subject><subject>Stereoisomerism</subject><subject>Structural analysis</subject><subject>Substrate Specificity</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOxDAQRS0EgmXhF5A7qoSZOC93oBUvCUEBFFSW40zAqyQGO7sSfD1eLdBSWbLP9cw9jJ0gpAhYni1Tu2ysG7RJMwCZYpYCwg6bYV3JBADELpsB5pjUKOCAHYawjLdlgfU-O4iREnKEGXtZvGmvzUTefunJupG7jms-ujX13PX21Q3xyfDH6_ubRPvPnkJkdSDeeTfwRzs6_2a_XGNXAx-ot72bLEfI8IjtdboPdPxzztnz1eXT4ia5e7i-XVzcJUaU1ZRIzGXeGiPzpq4LwE4gCdnUWSFklcUCtdQCu1oKg0UVMeqwyKqWZFGYHCsxZ6fbf9-9-1jF9dRgg6G-1yO5VVCVEAUKASKS5ZY03oXgqVPv3g6xlEJQG6tqqX6tqo1VhZmKVmPw5GfEqhmo_Yv9aozA-RagWHRtyatgLI2GWuvJTKp19r8Z3wRiiow</recordid><startdate>20100301</startdate><enddate>20100301</enddate><creator>Hwang, Heejin</creator><creator>Kim, SeungBum</creator><creator>Yoon, Sangyoung</creator><creator>Ryu, Yeonwoo</creator><creator>Lee, Sang Yoon</creator><creator>Kim, T. Doohun</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>20100301</creationdate><title>Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021</title><author>Hwang, Heejin ; Kim, SeungBum ; Yoon, Sangyoung ; Ryu, Yeonwoo ; Lee, Sang Yoon ; Kim, T. Doohun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c367t-91494dcc94b88501f31e39b825397214189a31f893c157c94ef1527de955c4173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Carboxylic Ester Hydrolases - ultrastructure</topic><topic>Circular Dichroism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Assays</topic><topic>Light</topic><topic>Molecular Sequence Data</topic><topic>p-Nitrophenyl acetate</topic><topic>Protein Conformation</topic><topic>Scattering, Radiation</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, Protein</topic><topic>SGNH-arylesterase</topic><topic>Sinorhizobium meliloti - enzymology</topic><topic>Solvents</topic><topic>Spectrometry, Fluorescence</topic><topic>Staining and Labeling</topic><topic>Stereoisomerism</topic><topic>Structural analysis</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hwang, Heejin</creatorcontrib><creatorcontrib>Kim, SeungBum</creatorcontrib><creatorcontrib>Yoon, Sangyoung</creatorcontrib><creatorcontrib>Ryu, Yeonwoo</creatorcontrib><creatorcontrib>Lee, Sang Yoon</creatorcontrib><creatorcontrib>Kim, T. Doohun</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>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hwang, Heejin</au><au>Kim, SeungBum</au><au>Yoon, Sangyoung</au><au>Ryu, Yeonwoo</au><au>Lee, Sang Yoon</au><au>Kim, T. Doohun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2010-03-01</date><risdate>2010</risdate><volume>46</volume><issue>2</issue><spage>145</spage><epage>152</epage><pages>145-152</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>A novel oligomeric SGNH-arylesterase (Sm23) from
Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser
10, Asp
187, and His
190) and oxyanion holes (Ser
10-Gly
50-Asn
90). The wild type enzyme was able to hydrolyze
p-nitrophenyl acetate, α- and β-naphthyl acetate, while S10A mutant completely lost its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. Furthermore, spherical or globular aggregates were observed with 1-butyl-3-methylimidazolium tetrafluoroborate, while amorphous aggregates were formed with 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>20060410</pmid><doi>10.1016/j.ijbiomac.2009.12.010</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - metabolism Carboxylic Ester Hydrolases - ultrastructure Circular Dichroism Electrophoresis, Polyacrylamide Gel Enzyme Assays Light Molecular Sequence Data p-Nitrophenyl acetate Protein Conformation Scattering, Radiation Sequence Alignment Sequence Analysis, Protein SGNH-arylesterase Sinorhizobium meliloti - enzymology Solvents Spectrometry, Fluorescence Staining and Labeling Stereoisomerism Structural analysis Substrate Specificity |
| title | Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021 |
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