Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties
To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different chang...
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Veröffentlicht in: | FEBS letters 1998-07, Vol.431 (2), p.255-258 |
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creator | Orth, Tatiana Voronov, Sergei Binevski, Petr Saenger, Wolfram Kost, Olga |
description | To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different changes of catalytic properties in the reaction of the hydrolysis of
N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme. |
doi_str_mv | 10.1016/S0014-5793(98)00767-4 |
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N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)00767-4</identifier><identifier>PMID: 9708914</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>ACE, angiotensin-converting enzyme ; Angiotensin-converting enzyme ; Animals ; Asialoenzyme ; Bovine lung ; Catalysis ; Cattle ; Cbz-Phe-His-Leu, carbobenzoxy-l-phenylalanyl-l-histidyl-l-leucine ; Deglycosylation ; Enzyme Stability ; FA-Phe-Ala-Arg, furanacryloyl-l-phenylalanyl-l-alanyl-l-arginine ; FA-Phe-Gly-Gly, furanacryloyl-l-phenylalanylglycylglycine ; FA-Phe-Phe-Arg, furanacryloyl-l-phenylalanyl-l-phenylalanyl-l-arginine ; Glycosylation ; Hip-His-Leu, hippuryl-l-histidyl-l-leucine ; Lung - enzymology ; N domain ; Peptidyl-Dipeptidase A - metabolism ; PNGase F, N-glycosidase F ; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis ; Substrate Specificity</subject><ispartof>FEBS letters, 1998-07, Vol.431 (2), p.255-258</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 431 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4724-1972383ee687500861085978fb3157a549e2f045c2fdee5d40ba8b210b704a6e3</citedby><cites>FETCH-LOGICAL-c4724-1972383ee687500861085978fb3157a549e2f045c2fdee5d40ba8b210b704a6e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2900767-4$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579398007674$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9708914$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orth, Tatiana</creatorcontrib><creatorcontrib>Voronov, Sergei</creatorcontrib><creatorcontrib>Binevski, Petr</creatorcontrib><creatorcontrib>Saenger, Wolfram</creatorcontrib><creatorcontrib>Kost, Olga</creatorcontrib><title>Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different changes of catalytic properties in the reaction of the hydrolysis of
N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme.</description><subject>ACE, angiotensin-converting enzyme</subject><subject>Angiotensin-converting enzyme</subject><subject>Animals</subject><subject>Asialoenzyme</subject><subject>Bovine lung</subject><subject>Catalysis</subject><subject>Cattle</subject><subject>Cbz-Phe-His-Leu, carbobenzoxy-l-phenylalanyl-l-histidyl-l-leucine</subject><subject>Deglycosylation</subject><subject>Enzyme Stability</subject><subject>FA-Phe-Ala-Arg, furanacryloyl-l-phenylalanyl-l-alanyl-l-arginine</subject><subject>FA-Phe-Gly-Gly, furanacryloyl-l-phenylalanylglycylglycine</subject><subject>FA-Phe-Phe-Arg, furanacryloyl-l-phenylalanyl-l-phenylalanyl-l-arginine</subject><subject>Glycosylation</subject><subject>Hip-His-Leu, hippuryl-l-histidyl-l-leucine</subject><subject>Lung - enzymology</subject><subject>N domain</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>PNGase F, N-glycosidase F</subject><subject>SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis</subject><subject>Substrate Specificity</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1P5CAYx4nZjTu6fgQTTmY9VKFAgdNmNb4lJnvY3TOh9Klh08JY2jH100tnJl71ROD_8jz8EDql5IISWl3-IYTyQkjNfmh1ToisZMEP0IoqyQrGK_UFrd4t39BRSv9JviuqD9GhlkRpyleovutmF9Pc2dHHgGOL67jxAfB66voY7DBjG558HCEkHwoXwwaG0YcnDOF17gH3sZlyGBL2Y8LOjrabR-_weojrxQnpO_ra2i7Byf48Rv9ub_5e3xePv-8ern89Fo7LkhdUy5IpBlApKQhRFSVKaKnamlEhreAaypZw4cq2ARANJ7VVdUlJLQm3FbBjdLbrzaOfJ0ij6X1y0HU2QJySkUyJzINlo9gZ3RBTGqA168H3-auGErOwNVu2ZgFntDJbtobn3Ol-wFT30Lyn9jCzfr_TX3wH8-dKze3NVblVFkGr7fNS9XNXBRnYxsNgkvMQHDR-ADeaJvoPln0Dukyesg</recordid><startdate>19980717</startdate><enddate>19980717</enddate><creator>Orth, Tatiana</creator><creator>Voronov, Sergei</creator><creator>Binevski, Petr</creator><creator>Saenger, Wolfram</creator><creator>Kost, Olga</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19980717</creationdate><title>Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties</title><author>Orth, Tatiana ; Voronov, Sergei ; Binevski, Petr ; Saenger, Wolfram ; Kost, Olga</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4724-1972383ee687500861085978fb3157a549e2f045c2fdee5d40ba8b210b704a6e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACE, angiotensin-converting enzyme</topic><topic>Angiotensin-converting enzyme</topic><topic>Animals</topic><topic>Asialoenzyme</topic><topic>Bovine lung</topic><topic>Catalysis</topic><topic>Cattle</topic><topic>Cbz-Phe-His-Leu, carbobenzoxy-l-phenylalanyl-l-histidyl-l-leucine</topic><topic>Deglycosylation</topic><topic>Enzyme Stability</topic><topic>FA-Phe-Ala-Arg, furanacryloyl-l-phenylalanyl-l-alanyl-l-arginine</topic><topic>FA-Phe-Gly-Gly, furanacryloyl-l-phenylalanylglycylglycine</topic><topic>FA-Phe-Phe-Arg, furanacryloyl-l-phenylalanyl-l-phenylalanyl-l-arginine</topic><topic>Glycosylation</topic><topic>Hip-His-Leu, hippuryl-l-histidyl-l-leucine</topic><topic>Lung - enzymology</topic><topic>N domain</topic><topic>Peptidyl-Dipeptidase A - metabolism</topic><topic>PNGase F, N-glycosidase F</topic><topic>SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orth, Tatiana</creatorcontrib><creatorcontrib>Voronov, Sergei</creatorcontrib><creatorcontrib>Binevski, Petr</creatorcontrib><creatorcontrib>Saenger, Wolfram</creatorcontrib><creatorcontrib>Kost, Olga</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orth, Tatiana</au><au>Voronov, Sergei</au><au>Binevski, Petr</au><au>Saenger, Wolfram</au><au>Kost, Olga</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-07-17</date><risdate>1998</risdate><volume>431</volume><issue>2</issue><spage>255</spage><epage>258</epage><pages>255-258</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different changes of catalytic properties in the reaction of the hydrolysis of
N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9708914</pmid><doi>10.1016/S0014-5793(98)00767-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | ACE, angiotensin-converting enzyme Angiotensin-converting enzyme Animals Asialoenzyme Bovine lung Catalysis Cattle Cbz-Phe-His-Leu, carbobenzoxy-l-phenylalanyl-l-histidyl-l-leucine Deglycosylation Enzyme Stability FA-Phe-Ala-Arg, furanacryloyl-l-phenylalanyl-l-alanyl-l-arginine FA-Phe-Gly-Gly, furanacryloyl-l-phenylalanylglycylglycine FA-Phe-Phe-Arg, furanacryloyl-l-phenylalanyl-l-phenylalanyl-l-arginine Glycosylation Hip-His-Leu, hippuryl-l-histidyl-l-leucine Lung - enzymology N domain Peptidyl-Dipeptidase A - metabolism PNGase F, N-glycosidase F SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis Substrate Specificity |
title | Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties |
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