Time-resolved solid-state REDOR NMR studies of UDP N-acetylglucosamine enolpyruvyl transferase
The new method of time-resolved solid-state rotational echo double resonance (REDOR) NMR spectroscopy introduced recently by this laboratory has been applied to the enzyme uridine N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase (EPT), with the goal of probing the interactions between reactive...
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| Veröffentlicht in: | FEBS letters 1995-12, Vol.377 (2), p.208-212 |
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| creator | Li, Yan Krekel, Florian Ramilo, Cecilia A. Amrhein, Nikolaus Evans, Jeremy N.S. |
| description | The new method of time-resolved solid-state rotational echo double resonance (REDOR) NMR spectroscopy introduced recently by this laboratory has been applied to the enzyme uridine
N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase (EPT), with the goal of probing the interactions between reactive species and their enzyme active site. The approach has been used in a qualitative fashion with the enzyme-inhibitor and enzyme-intermediate complexes of uniformly
15N-labeled UDP-NAG EPT, trapped under steady-state and pre-steady-state conditions. A different set of intermolecular interactions between the substrates UDP-NAG, UDP-NAG plus 3-
Z-fluorophosphoenolpyruvate, covalent
O-phosphothioketal, and UDP-NAG plus phosphoenolpyruvate trapped under time-resolved conditions (after 50 ms reaction time), and the EPT enzyme active site were observed, and this is contrasted to a similar study of the interactions in a related enzyme, 5-enolpyruvyl-shikimate-3-phosphate synthase. |
| doi_str_mv | 10.1016/0014-5793(95)01338-5 |
| format | Article |
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N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase (EPT), with the goal of probing the interactions between reactive species and their enzyme active site. The approach has been used in a qualitative fashion with the enzyme-inhibitor and enzyme-intermediate complexes of uniformly
15N-labeled UDP-NAG EPT, trapped under steady-state and pre-steady-state conditions. A different set of intermolecular interactions between the substrates UDP-NAG, UDP-NAG plus 3-
Z-fluorophosphoenolpyruvate, covalent
O-phosphothioketal, and UDP-NAG plus phosphoenolpyruvate trapped under time-resolved conditions (after 50 ms reaction time), and the EPT enzyme active site were observed, and this is contrasted to a similar study of the interactions in a related enzyme, 5-enolpyruvyl-shikimate-3-phosphate synthase.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)01338-5</identifier><identifier>PMID: 8543052</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>3-[N-morpholino]propanesulfonic acid ; 5-enolpyruvylshikimate-3-phosphate ; Alkyl and Aryl Transferases ; Binding Sites ; dithiothreitol ; DTT ; Enolpyruvyl transferase ; Enzyme active site ; Enzyme mechanism ; EPSP ; EPT ; Magnetic Resonance Spectroscopy ; Molecular Structure ; MOPS ; PEP ; phosphoenolpyruvate ; REDOR ; Rotational echo double resonance ; Substrate Specificity ; Time-resolved solid-state NMR ; Transferases - chemistry ; Transferases - metabolism ; UDP-NAG ; uridine diphosphate N-acetylglucosamine ; Uridine Diphosphate N-Acetylglucosamine - analogs & derivatives ; Uridine Diphosphate N-Acetylglucosamine - chemistry ; Uridine Diphosphate N-Acetylglucosamine - metabolism ; Uridine diphosphate N-acetylglucosamine enolpyruvyl transferase</subject><ispartof>FEBS letters, 1995-12, Vol.377 (2), p.208-212</ispartof><rights>1995</rights><rights>FEBS Letters 377 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4665-4422384865b0592b851965404b2183c14bfc71fcccc9fdebb9759a8ad240fb9b3</citedby><cites>FETCH-LOGICAL-c4665-4422384865b0592b851965404b2183c14bfc71fcccc9fdebb9759a8ad240fb9b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)01338-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8543052$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yan</creatorcontrib><creatorcontrib>Krekel, Florian</creatorcontrib><creatorcontrib>Ramilo, Cecilia A.</creatorcontrib><creatorcontrib>Amrhein, Nikolaus</creatorcontrib><creatorcontrib>Evans, Jeremy N.S.</creatorcontrib><title>Time-resolved solid-state REDOR NMR studies of UDP N-acetylglucosamine enolpyruvyl transferase</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The new method of time-resolved solid-state rotational echo double resonance (REDOR) NMR spectroscopy introduced recently by this laboratory has been applied to the enzyme uridine
N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase (EPT), with the goal of probing the interactions between reactive species and their enzyme active site. The approach has been used in a qualitative fashion with the enzyme-inhibitor and enzyme-intermediate complexes of uniformly
15N-labeled UDP-NAG EPT, trapped under steady-state and pre-steady-state conditions. A different set of intermolecular interactions between the substrates UDP-NAG, UDP-NAG plus 3-
Z-fluorophosphoenolpyruvate, covalent
O-phosphothioketal, and UDP-NAG plus phosphoenolpyruvate trapped under time-resolved conditions (after 50 ms reaction time), and the EPT enzyme active site were observed, and this is contrasted to a similar study of the interactions in a related enzyme, 5-enolpyruvyl-shikimate-3-phosphate synthase.</description><subject>3-[N-morpholino]propanesulfonic acid</subject><subject>5-enolpyruvylshikimate-3-phosphate</subject><subject>Alkyl and Aryl Transferases</subject><subject>Binding Sites</subject><subject>dithiothreitol</subject><subject>DTT</subject><subject>Enolpyruvyl transferase</subject><subject>Enzyme active site</subject><subject>Enzyme mechanism</subject><subject>EPSP</subject><subject>EPT</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Structure</subject><subject>MOPS</subject><subject>PEP</subject><subject>phosphoenolpyruvate</subject><subject>REDOR</subject><subject>Rotational echo double resonance</subject><subject>Substrate Specificity</subject><subject>Time-resolved solid-state NMR</subject><subject>Transferases - chemistry</subject><subject>Transferases - metabolism</subject><subject>UDP-NAG</subject><subject>uridine diphosphate N-acetylglucosamine</subject><subject>Uridine Diphosphate N-Acetylglucosamine - analogs & derivatives</subject><subject>Uridine Diphosphate N-Acetylglucosamine - chemistry</subject><subject>Uridine Diphosphate N-Acetylglucosamine - metabolism</subject><subject>Uridine diphosphate N-acetylglucosamine enolpyruvyl transferase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFv1DAQhS1EVZbCPwDJJ1QOLnZsJ_YFiba7gFRatGqvWLYzQUZOstjJovx7ku6qR8RcRjPvzbP1IfSG0QtGWfmBUiaIrDQ_1_I9ZZwrIp-hFVMVJ1yU6jlaPVleoJc5_6LzrJg-RadKCk5lsUI_7kMLJEHu4x5qPLdQkzzYAfB2fX23xbfftjgPYx0g477BD9ff8S2xHoYp_oyj77NtQwcYuj7upjTup4iHZLvcQLIZXqGTxsYMr4_9DD1s1vdXX8jN3eevV59uiBdlKYkQRcGVUKV0VOrCKcl0KQUVrmCKeyZc4yvW-Ll0U4NzupLaKlsXgjZOO36G3h1yd6n_PUIeTBuyhxhtB_2YTVVVqhJKzEZxMPrU55ygMbsUWpsmw6hZsJqFmVmYGS3NI1Yj57O3x_zRtVA_HR05zvrmoP8JEab_yjSb9WWxCMtey8ft8tDHQxDMtPYBksk-QOehDgn8YOo-_PunfwFdIZnr</recordid><startdate>19951218</startdate><enddate>19951218</enddate><creator>Li, Yan</creator><creator>Krekel, Florian</creator><creator>Ramilo, Cecilia A.</creator><creator>Amrhein, Nikolaus</creator><creator>Evans, Jeremy N.S.</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>19951218</creationdate><title>Time-resolved solid-state REDOR NMR studies of UDP N-acetylglucosamine enolpyruvyl transferase</title><author>Li, Yan ; Krekel, Florian ; Ramilo, Cecilia A. ; Amrhein, Nikolaus ; Evans, Jeremy N.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4665-4422384865b0592b851965404b2183c14bfc71fcccc9fdebb9759a8ad240fb9b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>3-[N-morpholino]propanesulfonic acid</topic><topic>5-enolpyruvylshikimate-3-phosphate</topic><topic>Alkyl and Aryl Transferases</topic><topic>Binding Sites</topic><topic>dithiothreitol</topic><topic>DTT</topic><topic>Enolpyruvyl transferase</topic><topic>Enzyme active site</topic><topic>Enzyme mechanism</topic><topic>EPSP</topic><topic>EPT</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Structure</topic><topic>MOPS</topic><topic>PEP</topic><topic>phosphoenolpyruvate</topic><topic>REDOR</topic><topic>Rotational echo double resonance</topic><topic>Substrate Specificity</topic><topic>Time-resolved solid-state NMR</topic><topic>Transferases - chemistry</topic><topic>Transferases - metabolism</topic><topic>UDP-NAG</topic><topic>uridine diphosphate N-acetylglucosamine</topic><topic>Uridine Diphosphate N-Acetylglucosamine - analogs & derivatives</topic><topic>Uridine Diphosphate N-Acetylglucosamine - chemistry</topic><topic>Uridine Diphosphate N-Acetylglucosamine - metabolism</topic><topic>Uridine diphosphate N-acetylglucosamine enolpyruvyl transferase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yan</creatorcontrib><creatorcontrib>Krekel, Florian</creatorcontrib><creatorcontrib>Ramilo, Cecilia A.</creatorcontrib><creatorcontrib>Amrhein, Nikolaus</creatorcontrib><creatorcontrib>Evans, Jeremy N.S.</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>Li, Yan</au><au>Krekel, Florian</au><au>Ramilo, Cecilia A.</au><au>Amrhein, Nikolaus</au><au>Evans, Jeremy N.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Time-resolved solid-state REDOR NMR studies of UDP N-acetylglucosamine enolpyruvyl transferase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-12-18</date><risdate>1995</risdate><volume>377</volume><issue>2</issue><spage>208</spage><epage>212</epage><pages>208-212</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The new method of time-resolved solid-state rotational echo double resonance (REDOR) NMR spectroscopy introduced recently by this laboratory has been applied to the enzyme uridine
N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase (EPT), with the goal of probing the interactions between reactive species and their enzyme active site. The approach has been used in a qualitative fashion with the enzyme-inhibitor and enzyme-intermediate complexes of uniformly
15N-labeled UDP-NAG EPT, trapped under steady-state and pre-steady-state conditions. A different set of intermolecular interactions between the substrates UDP-NAG, UDP-NAG plus 3-
Z-fluorophosphoenolpyruvate, covalent
O-phosphothioketal, and UDP-NAG plus phosphoenolpyruvate trapped under time-resolved conditions (after 50 ms reaction time), and the EPT enzyme active site were observed, and this is contrasted to a similar study of the interactions in a related enzyme, 5-enolpyruvyl-shikimate-3-phosphate synthase.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8543052</pmid><doi>10.1016/0014-5793(95)01338-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1995-12, Vol.377 (2), p.208-212 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 3-[N-morpholino]propanesulfonic acid 5-enolpyruvylshikimate-3-phosphate Alkyl and Aryl Transferases Binding Sites dithiothreitol DTT Enolpyruvyl transferase Enzyme active site Enzyme mechanism EPSP EPT Magnetic Resonance Spectroscopy Molecular Structure MOPS PEP phosphoenolpyruvate REDOR Rotational echo double resonance Substrate Specificity Time-resolved solid-state NMR Transferases - chemistry Transferases - metabolism UDP-NAG uridine diphosphate N-acetylglucosamine Uridine Diphosphate N-Acetylglucosamine - analogs & derivatives Uridine Diphosphate N-Acetylglucosamine - chemistry Uridine Diphosphate N-Acetylglucosamine - metabolism Uridine diphosphate N-acetylglucosamine enolpyruvyl transferase |
| title | Time-resolved solid-state REDOR NMR studies of UDP N-acetylglucosamine enolpyruvyl transferase |
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