Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin
Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpin from Gloeobacter violaceus that we named vioserp...
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| Veröffentlicht in: | Biochimie 2016-08, Vol.127, p.115-120 |
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| creator | Oliveira, Jocélia P.C. Salazar, Natália Zani, Marcelo B. de Souza, Lucas R. Passos, Silvia G. Sant'Ana, Aquiles M. de Andrade, Regiane A. Marcili, Arlei Sperança, Marcia A. Puzer, Luciano |
| description | Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpin from Gloeobacter violaceus that we named vioserpin. The serpin presented a high specificity to inhibit trypsin-like enzymes with a rapid inhibition rate constant (2.1 × 106 M−1 s−1). We also demonstrated that the inhibitory activity of the vioserpin is influenced by the concentration of heparin, and this finding may throw a new light on understanding the molecular evolution of serpins.
•Biochemical characterization of the vioserpin, a serine protease inhibitor from the bacteria Gloeobacter violaceus•The vioserpin inhibits specifically trypsin-like enzymes, with a very high second-order rate constant.•Vioserpin is modulated by glycosaminoglycans, a characteristic found in serpins from eukaryotic organisms only.•The phylogenetic studies point for a new branch of the serpin superfamily in prokaryotes. |
| doi_str_mv | 10.1016/j.biochi.2016.05.006 |
| format | Article |
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•Biochemical characterization of the vioserpin, a serine protease inhibitor from the bacteria Gloeobacter violaceus•The vioserpin inhibits specifically trypsin-like enzymes, with a very high second-order rate constant.•Vioserpin is modulated by glycosaminoglycans, a characteristic found in serpins from eukaryotic organisms only.•The phylogenetic studies point for a new branch of the serpin superfamily in prokaryotes.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2016.05.006</identifier><identifier>PMID: 27157268</identifier><language>eng</language><publisher>France: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Bacterial serpin ; Cattle ; Cyanobacteria ; Gloeobacter violaceus ; Heparin - metabolism ; Humans ; Kinetics ; Mice ; Phylogeny ; Protease inhibitor ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology ; Serine peptidase ; Serine Proteinase Inhibitors - chemistry ; Serine Proteinase Inhibitors - isolation & purification ; Serine Proteinase Inhibitors - metabolism ; Serine Proteinase Inhibitors - pharmacology ; Serpin ; Trypsin - metabolism ; Vioserpin</subject><ispartof>Biochimie, 2016-08, Vol.127, p.115-120</ispartof><rights>2016 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)</rights><rights>Copyright © 2016 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-14e0aade8c1d59ca85f790463e30e1c44398c856731163e3bb59c25253d29bdf3</citedby><cites>FETCH-LOGICAL-c362t-14e0aade8c1d59ca85f790463e30e1c44398c856731163e3bb59c25253d29bdf3</cites><orcidid>0000-0002-4412-0974</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biochi.2016.05.006$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27157268$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oliveira, Jocélia P.C.</creatorcontrib><creatorcontrib>Salazar, Natália</creatorcontrib><creatorcontrib>Zani, Marcelo B.</creatorcontrib><creatorcontrib>de Souza, Lucas R.</creatorcontrib><creatorcontrib>Passos, Silvia G.</creatorcontrib><creatorcontrib>Sant'Ana, Aquiles M.</creatorcontrib><creatorcontrib>de Andrade, Regiane A.</creatorcontrib><creatorcontrib>Marcili, Arlei</creatorcontrib><creatorcontrib>Sperança, Marcia A.</creatorcontrib><creatorcontrib>Puzer, Luciano</creatorcontrib><title>Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpin from Gloeobacter violaceus that we named vioserpin. The serpin presented a high specificity to inhibit trypsin-like enzymes with a rapid inhibition rate constant (2.1 × 106 M−1 s−1). We also demonstrated that the inhibitory activity of the vioserpin is influenced by the concentration of heparin, and this finding may throw a new light on understanding the molecular evolution of serpins.
•Biochemical characterization of the vioserpin, a serine protease inhibitor from the bacteria Gloeobacter violaceus•The vioserpin inhibits specifically trypsin-like enzymes, with a very high second-order rate constant.•Vioserpin is modulated by glycosaminoglycans, a characteristic found in serpins from eukaryotic organisms only.•The phylogenetic studies point for a new branch of the serpin superfamily in prokaryotes.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacterial serpin</subject><subject>Cattle</subject><subject>Cyanobacteria</subject><subject>Gloeobacter violaceus</subject><subject>Heparin - metabolism</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Phylogeny</subject><subject>Protease inhibitor</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Serine peptidase</subject><subject>Serine Proteinase Inhibitors - chemistry</subject><subject>Serine Proteinase Inhibitors - isolation & purification</subject><subject>Serine Proteinase Inhibitors - metabolism</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Serpin</subject><subject>Trypsin - metabolism</subject><subject>Vioserpin</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtP4zAQgC20CMrjHyDk4x42YRzHrnNBQmh5SEhcgKtlOxPqKo2DnSD13-OqsMc9eTz65vURcsGgZMDk1bq0PriVL6v8K0GUAPKALJjkqpBM8V9kARygaEDVx-QkpTUACKiaI3JcLZlYVlItiH7zIWEc_fCHGpojPyAdY5jQJKR-WHnrpxBpF8OG3vcBgzVuwkg_feiNwznRMaTkbb-lEd_n3kzYUrulKxxNbnZGDjvTJzz_fk_J693fl9uH4un5_vH25qlwXFZTwWoEY1pUjrWicUaJbtlALTlyQObqmjfKKSGXnLFd0tpMVaISvK0a23b8lPze9827f8yYJr3xyWHfmwHDnDRTwJRktVIZrfeoi3nziJ0eo9-YuNUM9E6tXuu9Wr1Tq0HorDaXXX5PmO0G239FPy4zcL0HMN_56THq5DwODlsf0U26Df7_E74AFyCM9A</recordid><startdate>201608</startdate><enddate>201608</enddate><creator>Oliveira, Jocélia P.C.</creator><creator>Salazar, Natália</creator><creator>Zani, Marcelo B.</creator><creator>de Souza, Lucas R.</creator><creator>Passos, Silvia G.</creator><creator>Sant'Ana, Aquiles M.</creator><creator>de Andrade, Regiane A.</creator><creator>Marcili, Arlei</creator><creator>Sperança, Marcia A.</creator><creator>Puzer, Luciano</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><orcidid>https://orcid.org/0000-0002-4412-0974</orcidid></search><sort><creationdate>201608</creationdate><title>Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin</title><author>Oliveira, Jocélia P.C. ; Salazar, Natália ; Zani, Marcelo B. ; de Souza, Lucas R. ; Passos, Silvia G. ; Sant'Ana, Aquiles M. ; de Andrade, Regiane A. ; Marcili, Arlei ; Sperança, Marcia A. ; Puzer, Luciano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-14e0aade8c1d59ca85f790463e30e1c44398c856731163e3bb59c25253d29bdf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacterial serpin</topic><topic>Cattle</topic><topic>Cyanobacteria</topic><topic>Gloeobacter violaceus</topic><topic>Heparin - metabolism</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Phylogeny</topic><topic>Protease inhibitor</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Serine peptidase</topic><topic>Serine Proteinase Inhibitors - chemistry</topic><topic>Serine Proteinase Inhibitors - isolation & purification</topic><topic>Serine Proteinase Inhibitors - metabolism</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Serpin</topic><topic>Trypsin - metabolism</topic><topic>Vioserpin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oliveira, Jocélia P.C.</creatorcontrib><creatorcontrib>Salazar, Natália</creatorcontrib><creatorcontrib>Zani, Marcelo B.</creatorcontrib><creatorcontrib>de Souza, Lucas R.</creatorcontrib><creatorcontrib>Passos, Silvia G.</creatorcontrib><creatorcontrib>Sant'Ana, Aquiles M.</creatorcontrib><creatorcontrib>de Andrade, Regiane A.</creatorcontrib><creatorcontrib>Marcili, Arlei</creatorcontrib><creatorcontrib>Sperança, Marcia A.</creatorcontrib><creatorcontrib>Puzer, Luciano</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>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oliveira, Jocélia P.C.</au><au>Salazar, Natália</au><au>Zani, Marcelo B.</au><au>de Souza, Lucas R.</au><au>Passos, Silvia G.</au><au>Sant'Ana, Aquiles M.</au><au>de Andrade, Regiane A.</au><au>Marcili, Arlei</au><au>Sperança, Marcia A.</au><au>Puzer, Luciano</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2016-08</date><risdate>2016</risdate><volume>127</volume><spage>115</spage><epage>120</epage><pages>115-120</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpin from Gloeobacter violaceus that we named vioserpin. The serpin presented a high specificity to inhibit trypsin-like enzymes with a rapid inhibition rate constant (2.1 × 106 M−1 s−1). We also demonstrated that the inhibitory activity of the vioserpin is influenced by the concentration of heparin, and this finding may throw a new light on understanding the molecular evolution of serpins.
•Biochemical characterization of the vioserpin, a serine protease inhibitor from the bacteria Gloeobacter violaceus•The vioserpin inhibits specifically trypsin-like enzymes, with a very high second-order rate constant.•Vioserpin is modulated by glycosaminoglycans, a characteristic found in serpins from eukaryotic organisms only.•The phylogenetic studies point for a new branch of the serpin superfamily in prokaryotes.</abstract><cop>France</cop><pub>Elsevier B.V</pub><pmid>27157268</pmid><doi>10.1016/j.biochi.2016.05.006</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-4412-0974</orcidid></addata></record> |
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| subjects | Amino Acid Sequence Animals Bacterial serpin Cattle Cyanobacteria Gloeobacter violaceus Heparin - metabolism Humans Kinetics Mice Phylogeny Protease inhibitor Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Recombinant Proteins - pharmacology Serine peptidase Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - isolation & purification Serine Proteinase Inhibitors - metabolism Serine Proteinase Inhibitors - pharmacology Serpin Trypsin - metabolism Vioserpin |
| title | Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin |
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