Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop
Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for mi...
Gespeichert in:
| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1989-04, Vol.244 (4900), p.82-85 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 85 |
|---|---|
| container_issue | 4900 |
| container_start_page | 82 |
| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 244 |
| creator | KUIPERS, O. P THUNNISJEN, M. M. G. M DE GEUS, P DIJKSTRA, B. W DRENTH, J VERHEIJ, H. M DE HAAS, G. H |
| description | Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected. |
| doi_str_mv | 10.1126/science.2704992 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_78925518</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A7552681</galeid><sourcerecordid>A7552681</sourcerecordid><originalsourceid>FETCH-LOGICAL-g560t-ae72318fd9de3b8fbc752ca358215c47ef56837553e788f1742038a3d34ea6af3</originalsourceid><addsrcrecordid>eNqN0s2L1DAUAPAiyjq7evYkFMH1sHbNR9Mkx3FYx4XBOfhx8VDepC-zWTJNbVpx_nuzbJFVBhxCCHnvxyMvSZa9oOSSUla9i8Zha_CSSVJqzR5lM0q0KDQj_HE2I4RXhSJSPM1OY7wlJOU0P8lOJj7Lvl-1N5AKNDmYwf10wz6HNm38gH0Kxg6Ns87cxYPNu5sQ0_Sug4j5nOWbfd6gx8GF9i4PeRx7CwZzH0L3LHtiwUd8Pq1n2dcPV18WH4vVenm9mK-KrajIUABKxqmyjW6Qb5TdGCmYAS4Uo8KUEq2oFJdCcJRKWSrL1JwC3vASoQLLz7Lz-7pdH36MGId656JB76HFMMZaKs2EoOq_kFelVqRiCb76B96GsW9TEzWjXHClpE7o4h5twWPtWhuGHswWW-zBhxatS-F5OjerFE367QGdRoM7Zw7wN3_xJAb8NWxhjLG-_vzpWLn-dqx8vzxSquXqobw4JE3wHrdYp3derB_ql9O9jpsdNnXXux30-3r6jin_espDNOBtn76mi38Y1ZzSUlD-G8OK6kk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>213538879</pqid></control><display><type>article</type><title>Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop</title><source>American Association for the Advancement of Science</source><source>Jstor Complete Legacy</source><source>MEDLINE</source><creator>KUIPERS, O. P ; THUNNISJEN, M. M. G. M ; DE GEUS, P ; DIJKSTRA, B. W ; DRENTH, J ; VERHEIJ, H. M ; DE HAAS, G. H</creator><creatorcontrib>KUIPERS, O. P ; THUNNISJEN, M. M. G. M ; DE GEUS, P ; DIJKSTRA, B. W ; DRENTH, J ; VERHEIJ, H. M ; DE HAAS, G. H</creatorcontrib><description>Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.2704992</identifier><identifier>PMID: 2704992</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Analysis ; Analytical, structural and metabolic biochemistry ; Animals ; Atomic structure ; Biological and medical sciences ; Crystallography ; Electronic structure ; Enzyme Activation ; Enzymes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrolases ; Kinetics ; Molecular Sequence Data ; Mutation ; Mutation (Biology) ; Pancreas - enzymology ; Phospholipases ; Phospholipases - metabolism ; Phospholipases A - genetics ; Phospholipases A - metabolism ; Phospholipases A - physiology ; Phospholipases A2 ; Protein Conformation ; Proteins ; Snake Venoms - analysis ; Structure-Activity Relationship ; Swine</subject><ispartof>Science (American Association for the Advancement of Science), 1989-04, Vol.244 (4900), p.82-85</ispartof><rights>1991 INIST-CNRS</rights><rights>COPYRIGHT 1989 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1989 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 7, 1989</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19311451$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2704992$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KUIPERS, O. P</creatorcontrib><creatorcontrib>THUNNISJEN, M. M. G. M</creatorcontrib><creatorcontrib>DE GEUS, P</creatorcontrib><creatorcontrib>DIJKSTRA, B. W</creatorcontrib><creatorcontrib>DRENTH, J</creatorcontrib><creatorcontrib>VERHEIJ, H. M</creatorcontrib><creatorcontrib>DE HAAS, G. H</creatorcontrib><title>Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.</description><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Atomic structure</subject><subject>Biological and medical sciences</subject><subject>Crystallography</subject><subject>Electronic structure</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolases</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Mutation (Biology)</subject><subject>Pancreas - enzymology</subject><subject>Phospholipases</subject><subject>Phospholipases - metabolism</subject><subject>Phospholipases A - genetics</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A - physiology</subject><subject>Phospholipases A2</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Snake Venoms - analysis</subject><subject>Structure-Activity Relationship</subject><subject>Swine</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0s2L1DAUAPAiyjq7evYkFMH1sHbNR9Mkx3FYx4XBOfhx8VDepC-zWTJNbVpx_nuzbJFVBhxCCHnvxyMvSZa9oOSSUla9i8Zha_CSSVJqzR5lM0q0KDQj_HE2I4RXhSJSPM1OY7wlJOU0P8lOJj7Lvl-1N5AKNDmYwf10wz6HNm38gH0Kxg6Ns87cxYPNu5sQ0_Sug4j5nOWbfd6gx8GF9i4PeRx7CwZzH0L3LHtiwUd8Pq1n2dcPV18WH4vVenm9mK-KrajIUABKxqmyjW6Qb5TdGCmYAS4Uo8KUEq2oFJdCcJRKWSrL1JwC3vASoQLLz7Lz-7pdH36MGId656JB76HFMMZaKs2EoOq_kFelVqRiCb76B96GsW9TEzWjXHClpE7o4h5twWPtWhuGHswWW-zBhxatS-F5OjerFE367QGdRoM7Zw7wN3_xJAb8NWxhjLG-_vzpWLn-dqx8vzxSquXqobw4JE3wHrdYp3derB_ql9O9jpsdNnXXux30-3r6jin_espDNOBtn76mi38Y1ZzSUlD-G8OK6kk</recordid><startdate>19890407</startdate><enddate>19890407</enddate><creator>KUIPERS, O. P</creator><creator>THUNNISJEN, M. M. G. M</creator><creator>DE GEUS, P</creator><creator>DIJKSTRA, B. W</creator><creator>DRENTH, J</creator><creator>VERHEIJ, H. M</creator><creator>DE HAAS, G. H</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19890407</creationdate><title>Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop</title><author>KUIPERS, O. P ; THUNNISJEN, M. M. G. M ; DE GEUS, P ; DIJKSTRA, B. W ; DRENTH, J ; VERHEIJ, H. M ; DE HAAS, G. H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g560t-ae72318fd9de3b8fbc752ca358215c47ef56837553e788f1742038a3d34ea6af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Atomic structure</topic><topic>Biological and medical sciences</topic><topic>Crystallography</topic><topic>Electronic structure</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolases</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Mutation (Biology)</topic><topic>Pancreas - enzymology</topic><topic>Phospholipases</topic><topic>Phospholipases - metabolism</topic><topic>Phospholipases A - genetics</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A - physiology</topic><topic>Phospholipases A2</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Snake Venoms - analysis</topic><topic>Structure-Activity Relationship</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KUIPERS, O. P</creatorcontrib><creatorcontrib>THUNNISJEN, M. M. G. M</creatorcontrib><creatorcontrib>DE GEUS, P</creatorcontrib><creatorcontrib>DIJKSTRA, B. W</creatorcontrib><creatorcontrib>DRENTH, J</creatorcontrib><creatorcontrib>VERHEIJ, H. M</creatorcontrib><creatorcontrib>DE HAAS, G. H</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>ProQuest Social Sciences Premium Collection</collection><collection>ProQuest Central (Corporate)</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Education Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Social Science Premium Collection</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Education Collection</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Civil Engineering Abstracts</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Agricultural Science Database</collection><collection>Education Database</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Education</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KUIPERS, O. P</au><au>THUNNISJEN, M. M. G. M</au><au>DE GEUS, P</au><au>DIJKSTRA, B. W</au><au>DRENTH, J</au><au>VERHEIJ, H. M</au><au>DE HAAS, G. H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1989-04-07</date><risdate>1989</risdate><volume>244</volume><issue>4900</issue><spage>82</spage><epage>85</epage><pages>82-85</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>2704992</pmid><doi>10.1126/science.2704992</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1989-04, Vol.244 (4900), p.82-85 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78925518 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amino Acid Sequence Analysis Analytical, structural and metabolic biochemistry Animals Atomic structure Biological and medical sciences Crystallography Electronic structure Enzyme Activation Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Kinetics Molecular Sequence Data Mutation Mutation (Biology) Pancreas - enzymology Phospholipases Phospholipases - metabolism Phospholipases A - genetics Phospholipases A - metabolism Phospholipases A - physiology Phospholipases A2 Protein Conformation Proteins Snake Venoms - analysis Structure-Activity Relationship Swine |
| title | Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T16%3A14%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enhanced%20activity%20and%20altered%20specificity%20of%20phospholipase%20A2%20by%20deletion%20of%20a%20surface%20loop&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=KUIPERS,%20O.%20P&rft.date=1989-04-07&rft.volume=244&rft.issue=4900&rft.spage=82&rft.epage=85&rft.pages=82-85&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.2704992&rft_dat=%3Cgale_proqu%3EA7552681%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213538879&rft_id=info:pmid/2704992&rft_galeid=A7552681&rfr_iscdi=true |