Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases
The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1997-03, Vol.404 (2), p.169-172 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 172 |
|---|---|
| container_issue | 2 |
| container_start_page | 169 |
| container_title | FEBS letters |
| container_volume | 404 |
| creator | Moiseyev, G.P Yakovlev, G.I Lysov, Yu.P Chernyi, A.A Polyakov, K.M Oivanen, M Lönnberg, H Beigelman, L.N Efimtseva, E.V Mikhailov, S.N |
| description | The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase A, RNase Pb
2, nuclease S
1 and snake venom phosphodiesterase. In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms. The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes.
©
1997 Federation of European Biochemical Societies. |
| doi_str_mv | 10.1016/S0014-5793(97)00092-6 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78872525</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579397000926</els_id><sourcerecordid>16282433</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5036-c344a9f0027ba0492a3a709cc29cbe3e15b3205b07323de5b86e3417a601e33</originalsourceid><addsrcrecordid>eNqNkc1u1TAQhS0EKpfCI1TKCsEiMLbjOF6htrQUqQKJsrccZyKMEvtiO4XL05Ofq27LypLPN2dG5xByRuEdBVq_vwOgVSmk4m-UfAsAipX1E7KjjeQlr-rmKdk9IM_Ji5R-zhBtqDohJ4pSBULuiP-IGePovMku-CL0Rf6BhZ_sgCG7DgsbfB_iuMnOr_I-hm6y2d1jgf7vYcQyTW3K0eSFH_cD_sG0eH37cl52uA_DzESTML0kz3ozJHx1fE_J3fXV98ub8vbrp8-X57elFcDr0vKqMqoHYLI1UClmuJGgrGXKtsiRipYzEC1IzniHom1q5BWVpgaKnJ-S15vrfOivCVPWo0sWh8F4DFPSsmkkE0w8CtKaNazii6PYQBtDShF7vY9uNPGgKeilDr3WoZestZJ6rUPX89zZccHUjtg9TB3zn_WbTf_tBjz8n6m-vrpgq7IISq7fy6oPmxXOud47jDpZh95i5yLarLvgHjn2H_4dr0M</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16282433</pqid></control><display><type>article</type><title>Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Access via Wiley Online Library</source><source>Access via ScienceDirect (Elsevier)</source><source>Wiley Online Library (Open Access Collection)</source><source>Alma/SFX Local Collection</source><creator>Moiseyev, G.P ; Yakovlev, G.I ; Lysov, Yu.P ; Chernyi, A.A ; Polyakov, K.M ; Oivanen, M ; Lönnberg, H ; Beigelman, L.N ; Efimtseva, E.V ; Mikhailov, S.N</creator><creatorcontrib>Moiseyev, G.P ; Yakovlev, G.I ; Lysov, Yu.P ; Chernyi, A.A ; Polyakov, K.M ; Oivanen, M ; Lönnberg, H ; Beigelman, L.N ; Efimtseva, E.V ; Mikhailov, S.N</creatorcontrib><description>The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase A, RNase Pb
2, nuclease S
1 and snake venom phosphodiesterase. In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms. The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes.
©
1997 Federation of European Biochemical Societies.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)00092-6</identifier><identifier>PMID: 9119057</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Calorimetry ; Cattle ; Conformation of substrate ; C′-methyl analogues of UpA ; Dinucleoside Phosphates - chemistry ; Dinucleoside Phosphates - metabolism ; Nucleic Acid Conformation ; Penicillium - enzymology ; Phosphoric Diester Hydrolases - chemistry ; Phosphoric Diester Hydrolases - metabolism ; Protein Conformation ; Ribonuclease, Pancreatic - chemistry ; Ribonuclease, Pancreatic - metabolism ; Ribonucleases - chemistry ; Ribonucleases - metabolism ; RNA-depolymerizing enzyme ; Single-Strand Specific DNA and RNA Endonucleases - chemistry ; Single-Strand Specific DNA and RNA Endonucleases - metabolism ; Snake Venoms</subject><ispartof>FEBS letters, 1997-03, Vol.404 (2), p.169-172</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 404 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5036-c344a9f0027ba0492a3a709cc29cbe3e15b3205b07323de5b86e3417a601e33</citedby><cites>FETCH-LOGICAL-c5036-c344a9f0027ba0492a3a709cc29cbe3e15b3205b07323de5b86e3417a601e33</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%2897%2900092-6$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(97)00092-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,782,786,1419,1435,3552,27931,27932,45581,45582,46002,46416,46840</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9119057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moiseyev, G.P</creatorcontrib><creatorcontrib>Yakovlev, G.I</creatorcontrib><creatorcontrib>Lysov, Yu.P</creatorcontrib><creatorcontrib>Chernyi, A.A</creatorcontrib><creatorcontrib>Polyakov, K.M</creatorcontrib><creatorcontrib>Oivanen, M</creatorcontrib><creatorcontrib>Lönnberg, H</creatorcontrib><creatorcontrib>Beigelman, L.N</creatorcontrib><creatorcontrib>Efimtseva, E.V</creatorcontrib><creatorcontrib>Mikhailov, S.N</creatorcontrib><title>Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase A, RNase Pb
2, nuclease S
1 and snake venom phosphodiesterase. In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms. The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes.
©
1997 Federation of European Biochemical Societies.</description><subject>Animals</subject><subject>Calorimetry</subject><subject>Cattle</subject><subject>Conformation of substrate</subject><subject>C′-methyl analogues of UpA</subject><subject>Dinucleoside Phosphates - chemistry</subject><subject>Dinucleoside Phosphates - metabolism</subject><subject>Nucleic Acid Conformation</subject><subject>Penicillium - enzymology</subject><subject>Phosphoric Diester Hydrolases - chemistry</subject><subject>Phosphoric Diester Hydrolases - metabolism</subject><subject>Protein Conformation</subject><subject>Ribonuclease, Pancreatic - chemistry</subject><subject>Ribonuclease, Pancreatic - metabolism</subject><subject>Ribonucleases - chemistry</subject><subject>Ribonucleases - metabolism</subject><subject>RNA-depolymerizing enzyme</subject><subject>Single-Strand Specific DNA and RNA Endonucleases - chemistry</subject><subject>Single-Strand Specific DNA and RNA Endonucleases - metabolism</subject><subject>Snake Venoms</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1TAQhS0EKpfCI1TKCsEiMLbjOF6htrQUqQKJsrccZyKMEvtiO4XL05Ofq27LypLPN2dG5xByRuEdBVq_vwOgVSmk4m-UfAsAipX1E7KjjeQlr-rmKdk9IM_Ji5R-zhBtqDohJ4pSBULuiP-IGePovMku-CL0Rf6BhZ_sgCG7DgsbfB_iuMnOr_I-hm6y2d1jgf7vYcQyTW3K0eSFH_cD_sG0eH37cl52uA_DzESTML0kz3ozJHx1fE_J3fXV98ub8vbrp8-X57elFcDr0vKqMqoHYLI1UClmuJGgrGXKtsiRipYzEC1IzniHom1q5BWVpgaKnJ-S15vrfOivCVPWo0sWh8F4DFPSsmkkE0w8CtKaNazii6PYQBtDShF7vY9uNPGgKeilDr3WoZestZJ6rUPX89zZccHUjtg9TB3zn_WbTf_tBjz8n6m-vrpgq7IISq7fy6oPmxXOud47jDpZh95i5yLarLvgHjn2H_4dr0M</recordid><startdate>19970310</startdate><enddate>19970310</enddate><creator>Moiseyev, G.P</creator><creator>Yakovlev, G.I</creator><creator>Lysov, Yu.P</creator><creator>Chernyi, A.A</creator><creator>Polyakov, K.M</creator><creator>Oivanen, M</creator><creator>Lönnberg, H</creator><creator>Beigelman, L.N</creator><creator>Efimtseva, E.V</creator><creator>Mikhailov, S.N</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19970310</creationdate><title>Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases</title><author>Moiseyev, G.P ; Yakovlev, G.I ; Lysov, Yu.P ; Chernyi, A.A ; Polyakov, K.M ; Oivanen, M ; Lönnberg, H ; Beigelman, L.N ; Efimtseva, E.V ; Mikhailov, S.N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5036-c344a9f0027ba0492a3a709cc29cbe3e15b3205b07323de5b86e3417a601e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Calorimetry</topic><topic>Cattle</topic><topic>Conformation of substrate</topic><topic>C′-methyl analogues of UpA</topic><topic>Dinucleoside Phosphates - chemistry</topic><topic>Dinucleoside Phosphates - metabolism</topic><topic>Nucleic Acid Conformation</topic><topic>Penicillium - enzymology</topic><topic>Phosphoric Diester Hydrolases - chemistry</topic><topic>Phosphoric Diester Hydrolases - metabolism</topic><topic>Protein Conformation</topic><topic>Ribonuclease, Pancreatic - chemistry</topic><topic>Ribonuclease, Pancreatic - metabolism</topic><topic>Ribonucleases - chemistry</topic><topic>Ribonucleases - metabolism</topic><topic>RNA-depolymerizing enzyme</topic><topic>Single-Strand Specific DNA and RNA Endonucleases - chemistry</topic><topic>Single-Strand Specific DNA and RNA Endonucleases - metabolism</topic><topic>Snake Venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moiseyev, G.P</creatorcontrib><creatorcontrib>Yakovlev, G.I</creatorcontrib><creatorcontrib>Lysov, Yu.P</creatorcontrib><creatorcontrib>Chernyi, A.A</creatorcontrib><creatorcontrib>Polyakov, K.M</creatorcontrib><creatorcontrib>Oivanen, M</creatorcontrib><creatorcontrib>Lönnberg, H</creatorcontrib><creatorcontrib>Beigelman, L.N</creatorcontrib><creatorcontrib>Efimtseva, E.V</creatorcontrib><creatorcontrib>Mikhailov, S.N</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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moiseyev, G.P</au><au>Yakovlev, G.I</au><au>Lysov, Yu.P</au><au>Chernyi, A.A</au><au>Polyakov, K.M</au><au>Oivanen, M</au><au>Lönnberg, H</au><au>Beigelman, L.N</au><au>Efimtseva, E.V</au><au>Mikhailov, S.N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-03-10</date><risdate>1997</risdate><volume>404</volume><issue>2</issue><spage>169</spage><epage>172</epage><pages>169-172</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase A, RNase Pb
2, nuclease S
1 and snake venom phosphodiesterase. In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms. The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes.
©
1997 Federation of European Biochemical Societies.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9119057</pmid><doi>10.1016/S0014-5793(97)00092-6</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1997-03, Vol.404 (2), p.169-172 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78872525 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | Animals Calorimetry Cattle Conformation of substrate C′-methyl analogues of UpA Dinucleoside Phosphates - chemistry Dinucleoside Phosphates - metabolism Nucleic Acid Conformation Penicillium - enzymology Phosphoric Diester Hydrolases - chemistry Phosphoric Diester Hydrolases - metabolism Protein Conformation Ribonuclease, Pancreatic - chemistry Ribonuclease, Pancreatic - metabolism Ribonucleases - chemistry Ribonucleases - metabolism RNA-depolymerizing enzyme Single-Strand Specific DNA and RNA Endonucleases - chemistry Single-Strand Specific DNA and RNA Endonucleases - metabolism Snake Venoms |
| title | Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-07T10%3A50%3A11IST&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=Determination%20of%20the%20nucleotide%20conformation%20in%20the%20productive%20enzyme-substrate%20complexes%20of%20RNA-depolymerases&rft.jtitle=FEBS%20letters&rft.au=Moiseyev,%20G.P&rft.date=1997-03-10&rft.volume=404&rft.issue=2&rft.spage=169&rft.epage=172&rft.pages=169-172&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/S0014-5793(97)00092-6&rft_dat=%3Cproquest_cross%3E16282433%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16282433&rft_id=info:pmid/9119057&rft_els_id=S0014579397000926&rfr_iscdi=true |