Loading…
Structure–function relationships in naturally occurring mutants of pancreatic lipase
From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic propert...
Saved in:
| Published in: | Protein engineering 1994-04, Vol.7 (4), p.563-569 |
|---|---|
| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c359t-f6f73354164e6e1907f1af1ef883b10d582fe462c272e9b0d59a6a314c8cd74c3 |
|---|---|
| cites | |
| container_end_page | 569 |
| container_issue | 4 |
| container_start_page | 563 |
| container_title | Protein engineering |
| container_volume | 7 |
| creator | CarriÈre, Frédéric Thirstrup, Kenneth Boel, Esper Verger, Robert Thim, Lars |
| description | From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic Upases. Both enzymes display a high phospholipase activity and are not interfaciaUy activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by mkeUar concentrations of bile salts and is not restored by addition of coUpase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic Upases, based on the closed and open conformations of the 3-D structure of human pancreatic Upase. |
| doi_str_mv | 10.1093/protein/7.4.563 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76586918</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76586918</sourcerecordid><originalsourceid>FETCH-LOGICAL-c359t-f6f73354164e6e1907f1af1ef883b10d582fe462c272e9b0d59a6a314c8cd74c3</originalsourceid><addsrcrecordid>eNo9kE2LFDEQhoMo67p69iT0Qbz1TCpJJ-mjDq4jrIj4wbKXkMlUNNqT7k3S4N78D_5Df4lZpplTvdT7VB0eQp4DXQHt-XpKY8EQ12olVp3kD8g5KAEtBS4enjKTj8mTnH9SyqQCOCNnmrKeAT8n3z6XNLsyJ_z356-foythjE3Cwd6H_CNMuQmxibYidhjumtG5OaUQvzeHudhYcjP6ZrLRJawnrhnCZDM-JY-8HTI-W-YF-Xr59stm2159fPd-8_qqdbzrS-ulV5x3AqRAidBT5cF6QK813wHdd5p5FJI5phj2u7rorbQchNNur4TjF-TV8W_1cDtjLuYQssNhsBHHORslOy170BVcH0GXxpwTejOlcLDpzgA19ybNYtIoI0w1WS9eLK_n3QH3J35RV_uXS2-zs4NP1UHIJ4z3mmsFFWuPWMgFf59qm34ZqbjqzPb6xlxffrh5s2WfzIb_B0kbj7M</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76586918</pqid></control><display><type>article</type><title>Structure–function relationships in naturally occurring mutants of pancreatic lipase</title><source>Oxford University Press Archive</source><creator>CarriÈre, Frédéric ; Thirstrup, Kenneth ; Boel, Esper ; Verger, Robert ; Thim, Lars</creator><creatorcontrib>CarriÈre, Frédéric ; Thirstrup, Kenneth ; Boel, Esper ; Verger, Robert ; Thim, Lars</creatorcontrib><description>From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic Upases. Both enzymes display a high phospholipase activity and are not interfaciaUy activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by mkeUar concentrations of bile salts and is not restored by addition of coUpase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic Upases, based on the closed and open conformations of the 3-D structure of human pancreatic Upase.</description><identifier>ISSN: 1741-0126</identifier><identifier>ISSN: 0269-2139</identifier><identifier>EISSN: 1741-0134</identifier><identifier>EISSN: 1460-213X</identifier><identifier>DOI: 10.1093/protein/7.4.563</identifier><identifier>PMID: 8029213</identifier><identifier>CODEN: PRENE9</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Aspergillus oryzae - genetics ; Biological and medical sciences ; Colipases - metabolism ; coypu ; Enzyme Activation ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; guinea pig ; Guinea Pigs ; Humans ; Hydrolases ; interfacial activation ; lid domain ; Lipase - chemistry ; Lipase - genetics ; Lipase - metabolism ; Lipase - ultrastructure ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutation ; phospholipase activity ; Phospholipases - analysis ; Recombinant Proteins - chemistry ; Rodentia ; Structure-Activity Relationship ; Triglycerides - metabolism</subject><ispartof>Protein engineering, 1994-04, Vol.7 (4), p.563-569</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c359t-f6f73354164e6e1907f1af1ef883b10d582fe462c272e9b0d59a6a314c8cd74c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3983871$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8029213$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CarriÈre, Frédéric</creatorcontrib><creatorcontrib>Thirstrup, Kenneth</creatorcontrib><creatorcontrib>Boel, Esper</creatorcontrib><creatorcontrib>Verger, Robert</creatorcontrib><creatorcontrib>Thim, Lars</creatorcontrib><title>Structure–function relationships in naturally occurring mutants of pancreatic lipase</title><title>Protein engineering</title><addtitle>Protein Eng</addtitle><description>From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic Upases. Both enzymes display a high phospholipase activity and are not interfaciaUy activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by mkeUar concentrations of bile salts and is not restored by addition of coUpase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic Upases, based on the closed and open conformations of the 3-D structure of human pancreatic Upase.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Aspergillus oryzae - genetics</subject><subject>Biological and medical sciences</subject><subject>Colipases - metabolism</subject><subject>coypu</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>guinea pig</subject><subject>Guinea Pigs</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>interfacial activation</subject><subject>lid domain</subject><subject>Lipase - chemistry</subject><subject>Lipase - genetics</subject><subject>Lipase - metabolism</subject><subject>Lipase - ultrastructure</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>phospholipase activity</subject><subject>Phospholipases - analysis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Rodentia</subject><subject>Structure-Activity Relationship</subject><subject>Triglycerides - metabolism</subject><issn>1741-0126</issn><issn>0269-2139</issn><issn>1741-0134</issn><issn>1460-213X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNo9kE2LFDEQhoMo67p69iT0Qbz1TCpJJ-mjDq4jrIj4wbKXkMlUNNqT7k3S4N78D_5Df4lZpplTvdT7VB0eQp4DXQHt-XpKY8EQ12olVp3kD8g5KAEtBS4enjKTj8mTnH9SyqQCOCNnmrKeAT8n3z6XNLsyJ_z356-foythjE3Cwd6H_CNMuQmxibYidhjumtG5OaUQvzeHudhYcjP6ZrLRJawnrhnCZDM-JY-8HTI-W-YF-Xr59stm2159fPd-8_qqdbzrS-ulV5x3AqRAidBT5cF6QK813wHdd5p5FJI5phj2u7rorbQchNNur4TjF-TV8W_1cDtjLuYQssNhsBHHORslOy170BVcH0GXxpwTejOlcLDpzgA19ybNYtIoI0w1WS9eLK_n3QH3J35RV_uXS2-zs4NP1UHIJ4z3mmsFFWuPWMgFf59qm34ZqbjqzPb6xlxffrh5s2WfzIb_B0kbj7M</recordid><startdate>19940401</startdate><enddate>19940401</enddate><creator>CarriÈre, Frédéric</creator><creator>Thirstrup, Kenneth</creator><creator>Boel, Esper</creator><creator>Verger, Robert</creator><creator>Thim, Lars</creator><general>Oxford University Press</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19940401</creationdate><title>Structure–function relationships in naturally occurring mutants of pancreatic lipase</title><author>CarriÈre, Frédéric ; Thirstrup, Kenneth ; Boel, Esper ; Verger, Robert ; Thim, Lars</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c359t-f6f73354164e6e1907f1af1ef883b10d582fe462c272e9b0d59a6a314c8cd74c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Aspergillus oryzae - genetics</topic><topic>Biological and medical sciences</topic><topic>Colipases - metabolism</topic><topic>coypu</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>guinea pig</topic><topic>Guinea Pigs</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>interfacial activation</topic><topic>lid domain</topic><topic>Lipase - chemistry</topic><topic>Lipase - genetics</topic><topic>Lipase - metabolism</topic><topic>Lipase - ultrastructure</topic><topic>Models, Biological</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>phospholipase activity</topic><topic>Phospholipases - analysis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Rodentia</topic><topic>Structure-Activity Relationship</topic><topic>Triglycerides - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CarriÈre, Frédéric</creatorcontrib><creatorcontrib>Thirstrup, Kenneth</creatorcontrib><creatorcontrib>Boel, Esper</creatorcontrib><creatorcontrib>Verger, Robert</creatorcontrib><creatorcontrib>Thim, Lars</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><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>Protein engineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CarriÈre, Frédéric</au><au>Thirstrup, Kenneth</au><au>Boel, Esper</au><au>Verger, Robert</au><au>Thim, Lars</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure–function relationships in naturally occurring mutants of pancreatic lipase</atitle><jtitle>Protein engineering</jtitle><addtitle>Protein Eng</addtitle><date>1994-04-01</date><risdate>1994</risdate><volume>7</volume><issue>4</issue><spage>563</spage><epage>569</epage><pages>563-569</pages><issn>1741-0126</issn><issn>0269-2139</issn><eissn>1741-0134</eissn><eissn>1460-213X</eissn><coden>PRENE9</coden><abstract>From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic Upases. Both enzymes display a high phospholipase activity and are not interfaciaUy activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by mkeUar concentrations of bile salts and is not restored by addition of coUpase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic Upases, based on the closed and open conformations of the 3-D structure of human pancreatic Upase.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>8029213</pmid><doi>10.1093/protein/7.4.563</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1741-0126 |
| ispartof | Protein engineering, 1994-04, Vol.7 (4), p.563-569 |
| issn | 1741-0126 0269-2139 1741-0134 1460-213X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76586918 |
| source | Oxford University Press Archive |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Aspergillus oryzae - genetics Biological and medical sciences Colipases - metabolism coypu Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology guinea pig Guinea Pigs Humans Hydrolases interfacial activation lid domain Lipase - chemistry Lipase - genetics Lipase - metabolism Lipase - ultrastructure Models, Biological Models, Molecular Molecular Sequence Data Mutation phospholipase activity Phospholipases - analysis Recombinant Proteins - chemistry Rodentia Structure-Activity Relationship Triglycerides - metabolism |
| title | Structure–function relationships in naturally occurring mutants of pancreatic lipase |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T22%3A16%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%E2%80%93function%20relationships%20in%20naturally%20occurring%20mutants%20of%20pancreatic%20lipase&rft.jtitle=Protein%20engineering&rft.au=Carri%C3%88re,%20Fr%C3%A9d%C3%A9ric&rft.date=1994-04-01&rft.volume=7&rft.issue=4&rft.spage=563&rft.epage=569&rft.pages=563-569&rft.issn=1741-0126&rft.eissn=1741-0134&rft.coden=PRENE9&rft_id=info:doi/10.1093/protein/7.4.563&rft_dat=%3Cproquest_cross%3E76586918%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c359t-f6f73354164e6e1907f1af1ef883b10d582fe462c272e9b0d59a6a314c8cd74c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=76586918&rft_id=info:pmid/8029213&rfr_iscdi=true |