Structural characterization of Escherichia coli sialic acid synthase
Sialic acid synthase encoded by the neuB gene of Escherichia coli catalyzes the condensation of N-acetylmannosamine and phosphoenolpyruvate to form N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2002-07, Vol.295 (1), p.167-173 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Hwang, Tzann-Shun Hung, Chih-Hung Teo, Chin-Fen Chen, Guan-Ting Chang, Lee-Shang Chen, Sung-Fang Chen, Yu-Ju Lin, Chun-Hung |
| description | Sialic acid synthase encoded by the
neuB gene of
Escherichia coli catalyzes the condensation of
N-acetylmannosamine and phosphoenolpyruvate to form
N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking studies. Also, a specific cleavage by endogenous protease(s) has been identified at Lys
280 of the enzyme (40
kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7
kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quaternary structures. |
| doi_str_mv | 10.1016/S0006-291X(02)00620-4 |
| format | Article |
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neuB gene of
Escherichia coli catalyzes the condensation of
N-acetylmannosamine and phosphoenolpyruvate to form
N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking studies. Also, a specific cleavage by endogenous protease(s) has been identified at Lys
280 of the enzyme (40
kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7
kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quaternary structures.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(02)00620-4</identifier><identifier>PMID: 12083785</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aldehyde-Lyases - chemistry ; Circular Dichroism ; Circular dichroism (CD) ; Escherichia coli - enzymology ; Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF) ; N-Acetylneuraminic acid (NeuAc) ; Oxo-Acid-Lyases - chemistry ; Oxo-Acid-Lyases - metabolism ; Protein Conformation ; Sialic acid synthase ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Subunit cross-linking</subject><ispartof>Biochemical and biophysical research communications, 2002-07, Vol.295 (1), p.167-173</ispartof><rights>2002 Elsevier Science (USA)</rights><rights>(c) 2002 Elsevier Science (USA).</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-28650cea233600205a80265081fb8b968df11de029a71ad54ee12ed3921ae9353</citedby><cites>FETCH-LOGICAL-c439t-28650cea233600205a80265081fb8b968df11de029a71ad54ee12ed3921ae9353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(02)00620-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12083785$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hwang, Tzann-Shun</creatorcontrib><creatorcontrib>Hung, Chih-Hung</creatorcontrib><creatorcontrib>Teo, Chin-Fen</creatorcontrib><creatorcontrib>Chen, Guan-Ting</creatorcontrib><creatorcontrib>Chang, Lee-Shang</creatorcontrib><creatorcontrib>Chen, Sung-Fang</creatorcontrib><creatorcontrib>Chen, Yu-Ju</creatorcontrib><creatorcontrib>Lin, Chun-Hung</creatorcontrib><title>Structural characterization of Escherichia coli sialic acid synthase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Sialic acid synthase encoded by the
neuB gene of
Escherichia coli catalyzes the condensation of
N-acetylmannosamine and phosphoenolpyruvate to form
N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking studies. Also, a specific cleavage by endogenous protease(s) has been identified at Lys
280 of the enzyme (40
kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7
kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quaternary structures.</description><subject>Aldehyde-Lyases - chemistry</subject><subject>Circular Dichroism</subject><subject>Circular dichroism (CD)</subject><subject>Escherichia coli - enzymology</subject><subject>Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF)</subject><subject>N-Acetylneuraminic acid (NeuAc)</subject><subject>Oxo-Acid-Lyases - chemistry</subject><subject>Oxo-Acid-Lyases - metabolism</subject><subject>Protein Conformation</subject><subject>Sialic acid synthase</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Subunit cross-linking</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRbK3-BCUn0UN0ZvO1OYnU-gEFD1Xwtmw3E7KSJnV3I9Rfb_qBHnuaYXjemeFh7BzhBgHT2xkApCHP8eMK-HXfcwjjAzZEyCHkCPEhG_4hA3bi3CcAYpzmx2yAHESUiWTIHmbedtp3VtWBrpRV2pM1P8qbtgnaMpg4XfUDXRkV6LY2gTOqNjpQ2hSBWzW-Uo5O2VGpakdnuzpi74-Tt_FzOH19ehnfT0MdR7kPuUgT0KR4FKUAHBIlgPcjgeVczPNUFCViQcBzlaEqkpgIORVRzlFRHiXRiF1u9y5t-9WR83JhnKa6Vg21nZMZioRnKe4FUcQ87t_pwWQLats6Z6mUS2sWyq4kglx7lhvPci1RApcbzzLucxe7A918QcV_aie2B-62APU-vg1Z6bShRlNhLGkvi9bsOfELhqGMIg</recordid><startdate>20020705</startdate><enddate>20020705</enddate><creator>Hwang, Tzann-Shun</creator><creator>Hung, Chih-Hung</creator><creator>Teo, Chin-Fen</creator><creator>Chen, Guan-Ting</creator><creator>Chang, Lee-Shang</creator><creator>Chen, Sung-Fang</creator><creator>Chen, Yu-Ju</creator><creator>Lin, Chun-Hung</creator><general>Elsevier Inc</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20020705</creationdate><title>Structural characterization of Escherichia coli sialic acid synthase</title><author>Hwang, Tzann-Shun ; Hung, Chih-Hung ; Teo, Chin-Fen ; Chen, Guan-Ting ; Chang, Lee-Shang ; Chen, Sung-Fang ; Chen, Yu-Ju ; Lin, Chun-Hung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-28650cea233600205a80265081fb8b968df11de029a71ad54ee12ed3921ae9353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Aldehyde-Lyases - chemistry</topic><topic>Circular Dichroism</topic><topic>Circular dichroism (CD)</topic><topic>Escherichia coli - enzymology</topic><topic>Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF)</topic><topic>N-Acetylneuraminic acid (NeuAc)</topic><topic>Oxo-Acid-Lyases - chemistry</topic><topic>Oxo-Acid-Lyases - metabolism</topic><topic>Protein Conformation</topic><topic>Sialic acid synthase</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Subunit cross-linking</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hwang, Tzann-Shun</creatorcontrib><creatorcontrib>Hung, Chih-Hung</creatorcontrib><creatorcontrib>Teo, Chin-Fen</creatorcontrib><creatorcontrib>Chen, Guan-Ting</creatorcontrib><creatorcontrib>Chang, Lee-Shang</creatorcontrib><creatorcontrib>Chen, Sung-Fang</creatorcontrib><creatorcontrib>Chen, Yu-Ju</creatorcontrib><creatorcontrib>Lin, Chun-Hung</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hwang, Tzann-Shun</au><au>Hung, Chih-Hung</au><au>Teo, Chin-Fen</au><au>Chen, Guan-Ting</au><au>Chang, Lee-Shang</au><au>Chen, Sung-Fang</au><au>Chen, Yu-Ju</au><au>Lin, Chun-Hung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural characterization of Escherichia coli sialic acid synthase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2002-07-05</date><risdate>2002</risdate><volume>295</volume><issue>1</issue><spage>167</spage><epage>173</epage><pages>167-173</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Sialic acid synthase encoded by the
neuB gene of
Escherichia coli catalyzes the condensation of
N-acetylmannosamine and phosphoenolpyruvate to form
N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking studies. Also, a specific cleavage by endogenous protease(s) has been identified at Lys
280 of the enzyme (40
kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7
kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quaternary structures.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12083785</pmid><doi>10.1016/S0006-291X(02)00620-4</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| subjects | Aldehyde-Lyases - chemistry Circular Dichroism Circular dichroism (CD) Escherichia coli - enzymology Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF) N-Acetylneuraminic acid (NeuAc) Oxo-Acid-Lyases - chemistry Oxo-Acid-Lyases - metabolism Protein Conformation Sialic acid synthase Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Subunit cross-linking |
| title | Structural characterization of Escherichia coli sialic acid synthase |
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