Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136(T).
Identifieur interne : 002073 ( PubMed/Curation ); précédent : 002072; suivant : 002074Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136(T).
Auteurs : Kubra F. Naqvi [États-Unis] ; Delphine Patin [France] ; Matthew S. Wheatley [États-Unis] ; Michael A. Savka [États-Unis] ; Renwick C J. Dobson [Australie] ; Han Ming Gan [Malaisie] ; Hélène Barreteau [France] ; Didier Blanot [France] ; Dominique Mengin-Lecreulx [France] ; André O. Hudson [États-Unis]Source :
- Frontiers in microbiology [ 1664-302X ] ; 2016.
Abstract
The enzymes involved in synthesizing the bacterial cell wall are attractive targets for the design of antibacterial compounds, since this pathway is essential for bacteria and is absent in animals, particularly humans. A survey of the genome of a bacterium that belongs to the phylum Verrucomicrobia, the closest free-living relative to bacteria from the Chlamydiales phylum, shows genetic evidence that Verrucomicrobium spinosum possesses a novel fusion open reading frame (ORF) annotated by the locus tag (VspiD_010100018130). The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:l-alanine ligase (MurC) that are involved in the cytoplasmic steps of peptidoglycan biosynthesis, was cloned. In vivo analyses using functional complementation showed that the fusion gene was able to complement Escherichia coli murB and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/C Vs ) was shown to be endowed with UDP-N-acetylmuramate:l-alanine ligase activity. In vitro analyses demonstrated that the latter enzyme had a pH optimum of 9.0, a magnesium optimum of 10 mM and a temperature optimum of 44-46°C. Its apparent K m values for ATP, UDP-MurNAc, and l-alanine were 470, 90, and 25 μM, respectively. However, all attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity were unsuccessful. Lastly, Hidden Markov Model-based similarity search and phylogenetic analysis revealed that this fusion enzyme could only be identified in specific lineages within the Verrucomicrobia phylum.
DOI: 10.3389/fmicb.2016.00362
PubMed: 27047475
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136(T).</title><author><name sortKey="Naqvi, Kubra F" sort="Naqvi, Kubra F" uniqKey="Naqvi K" first="Kubra F" last="Naqvi">Kubra F. Naqvi</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. 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Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author><author><name sortKey="Savka, Michael A" sort="Savka, Michael A" uniqKey="Savka M" first="Michael A" last="Savka">Michael A. Savka</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author><author><name sortKey="Dobson, Renwick C J" sort="Dobson, Renwick C J" uniqKey="Dobson R" first="Renwick C J" last="Dobson">Renwick C J. 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Hudson</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27047475</idno><idno type="pmid">27047475</idno><idno type="doi">10.3389/fmicb.2016.00362</idno><idno type="wicri:Area/PubMed/Corpus">002098</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002098</idno><idno type="wicri:Area/PubMed/Curation">002073</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002073</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136(T).</title><author><name sortKey="Naqvi, Kubra F" sort="Naqvi, Kubra F" uniqKey="Naqvi K" first="Kubra F" last="Naqvi">Kubra F. Naqvi</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author><author><name sortKey="Patin, Delphine" sort="Patin, Delphine" uniqKey="Patin D" first="Delphine" last="Patin">Delphine Patin</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay</wicri:regionArea></affiliation></author><author><name sortKey="Wheatley, Matthew S" sort="Wheatley, Matthew S" uniqKey="Wheatley M" first="Matthew S" last="Wheatley">Matthew S. Wheatley</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author><author><name sortKey="Savka, Michael A" sort="Savka, Michael A" uniqKey="Savka M" first="Michael A" last="Savka">Michael A. Savka</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author><author><name sortKey="Dobson, Renwick C J" sort="Dobson, Renwick C J" uniqKey="Dobson R" first="Renwick C J" last="Dobson">Renwick C J. Dobson</name><affiliation wicri:level="1"><nlm:affiliation>Biomolecular Interaction Centre, School of Biological Sciences, University of CanterburyChristchurch, New Zealand; Department of Biochemistry and Molecular Biology, Bio21 Molecular and Biotechnology Institute, The University of MelbourneParkville, VIC, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Biomolecular Interaction Centre, School of Biological Sciences, University of CanterburyChristchurch, New Zealand; Department of Biochemistry and Molecular Biology, Bio21 Molecular and Biotechnology Institute, The University of MelbourneParkville, VIC</wicri:regionArea></affiliation></author><author><name sortKey="Gan, Han Ming" sort="Gan, Han Ming" uniqKey="Gan H" first="Han Ming" last="Gan">Han Ming Gan</name><affiliation wicri:level="1"><nlm:affiliation>Monash University Malaysia Genomics Facility, Monash University MalaysiaSelangor, Malaysia; School of Science, Monash University MalaysiaSelangor, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>Monash University Malaysia Genomics Facility, Monash University MalaysiaSelangor, Malaysia; School of Science, Monash University MalaysiaSelangor</wicri:regionArea></affiliation></author><author><name sortKey="Barreteau, Helene" sort="Barreteau, Helene" uniqKey="Barreteau H" first="Hélène" last="Barreteau">Hélène Barreteau</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay</wicri:regionArea></affiliation></author><author><name sortKey="Blanot, Didier" sort="Blanot, Didier" uniqKey="Blanot D" first="Didier" last="Blanot">Didier Blanot</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay</wicri:regionArea></affiliation></author><author><name sortKey="Mengin Lecreulx, Dominique" sort="Mengin Lecreulx, Dominique" uniqKey="Mengin Lecreulx D" first="Dominique" last="Mengin-Lecreulx">Dominique Mengin-Lecreulx</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay</wicri:regionArea></affiliation></author><author><name sortKey="Hudson, Andre O" sort="Hudson, Andre O" uniqKey="Hudson A" first="André O" last="Hudson">André O. Hudson</name><affiliation wicri:level="1"><nlm:affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY</wicri:regionArea></affiliation></author></analytic><series><title level="j">Frontiers in microbiology</title><idno type="ISSN">1664-302X</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The enzymes involved in synthesizing the bacterial cell wall are attractive targets for the design of antibacterial compounds, since this pathway is essential for bacteria and is absent in animals, particularly humans. A survey of the genome of a bacterium that belongs to the phylum Verrucomicrobia, the closest free-living relative to bacteria from the Chlamydiales phylum, shows genetic evidence that Verrucomicrobium spinosum possesses a novel fusion open reading frame (ORF) annotated by the locus tag (VspiD_010100018130). The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:l-alanine ligase (MurC) that are involved in the cytoplasmic steps of peptidoglycan biosynthesis, was cloned. In vivo analyses using functional complementation showed that the fusion gene was able to complement Escherichia coli murB and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/C Vs ) was shown to be endowed with UDP-N-acetylmuramate:l-alanine ligase activity. In vitro analyses demonstrated that the latter enzyme had a pH optimum of 9.0, a magnesium optimum of 10 mM and a temperature optimum of 44-46°C. Its apparent K m values for ATP, UDP-MurNAc, and l-alanine were 470, 90, and 25 μM, respectively. However, all attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity were unsuccessful. Lastly, Hidden Markov Model-based similarity search and phylogenetic analysis revealed that this fusion enzyme could only be identified in specific lineages within the Verrucomicrobia phylum.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">27047475</PMID><DateCreated><Year>2016</Year><Month>04</Month><Day>06</Day></DateCreated><DateCompleted><Year>2016</Year><Month>04</Month><Day>06</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-302X</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><PubDate><Year>2016</Year></PubDate></JournalIssue><Title>Frontiers in microbiology</Title><ISOAbbreviation>Front Microbiol</ISOAbbreviation></Journal><ArticleTitle>Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136(T).</ArticleTitle><Pagination><MedlinePgn>362</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fmicb.2016.00362</ELocationID><Abstract><AbstractText>The enzymes involved in synthesizing the bacterial cell wall are attractive targets for the design of antibacterial compounds, since this pathway is essential for bacteria and is absent in animals, particularly humans. A survey of the genome of a bacterium that belongs to the phylum Verrucomicrobia, the closest free-living relative to bacteria from the Chlamydiales phylum, shows genetic evidence that Verrucomicrobium spinosum possesses a novel fusion open reading frame (ORF) annotated by the locus tag (VspiD_010100018130). The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:l-alanine ligase (MurC) that are involved in the cytoplasmic steps of peptidoglycan biosynthesis, was cloned. In vivo analyses using functional complementation showed that the fusion gene was able to complement Escherichia coli murB and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/C Vs ) was shown to be endowed with UDP-N-acetylmuramate:l-alanine ligase activity. In vitro analyses demonstrated that the latter enzyme had a pH optimum of 9.0, a magnesium optimum of 10 mM and a temperature optimum of 44-46°C. Its apparent K m values for ATP, UDP-MurNAc, and l-alanine were 470, 90, and 25 μM, respectively. However, all attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity were unsuccessful. Lastly, Hidden Markov Model-based similarity search and phylogenetic analysis revealed that this fusion enzyme could only be identified in specific lineages within the Verrucomicrobia phylum.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Naqvi</LastName><ForeName>Kubra F</ForeName><Initials>KF</Initials><AffiliationInfo><Affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Patin</LastName><ForeName>Delphine</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wheatley</LastName><ForeName>Matthew S</ForeName><Initials>MS</Initials><AffiliationInfo><Affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Savka</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dobson</LastName><ForeName>Renwick C J</ForeName><Initials>RC</Initials><AffiliationInfo><Affiliation>Biomolecular Interaction Centre, School of Biological Sciences, University of CanterburyChristchurch, New Zealand; Department of Biochemistry and Molecular Biology, Bio21 Molecular and Biotechnology Institute, The University of MelbourneParkville, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Han Ming</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>Monash University Malaysia Genomics Facility, Monash University MalaysiaSelangor, Malaysia; School of Science, Monash University MalaysiaSelangor, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barreteau</LastName><ForeName>Hélène</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Blanot</LastName><ForeName>Didier</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mengin-Lecreulx</LastName><ForeName>Dominique</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay Orsay, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hudson</LastName><ForeName>André O</ForeName><Initials>AO</Initials><AffiliationInfo><Affiliation>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology Rochester, NY, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>03</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Microbiol</MedlineTA><NlmUniqueID>101548977</NlmUniqueID><ISSNLinking>1664-302X</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Bioinformatics. 2009 Aug 1;25(15):1972-3</RefSource><PMID Version="1">19505945</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2015 Sep 15;112(37):11660-5</RefSource><PMID Version="1">26290580</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2010 Mar 10;5(3):e9490</RefSource><PMID Version="1">20224823</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 1993 Mar 2;32(8):2024-30</RefSource><PMID Version="1">8448160</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Biol Evol. 2013 Apr;30(4):772-80</RefSource><PMID Version="1">23329690</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Environ Microbiol. 2004 Jun;6(6):611-21</RefSource><PMID Version="1">15142250</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Bioinformatics. 2011 Apr 1;27(7):1009-10</RefSource><PMID Version="1">21278367</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 1992 Apr 27;301(3):271-6</RefSource><PMID Version="1">1577165</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Microbiol Mol Biol Rev. 2005 Dec;69(4):585-607</RefSource><PMID Version="1">16339737</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Methods Enzymol. 2002;354:189-96</RefSource><PMID Version="1">12418226</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Microbiol. 2005 Jul;57(1):41-52</RefSource><PMID Version="1">15948948</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nucleic Acids Res. 2015 Jan;43(Database issue):D222-6</RefSource><PMID Version="1">25414356</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Front Microbiol. 2012 May 25;3:183</RefSource><PMID Version="1">22783236</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 1996 Feb 6;35(5):1417-22</RefSource><PMID Version="1">8634271</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 2003 Nov;185(22):6507-12</RefSource><PMID Version="1">14594822</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Commun. 2013;4:2304</RefSource><PMID Version="1">23942190</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nucleic Acids Res. 2003 Jan 1;31(1):371-3</RefSource><PMID Version="1">12520025</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Front Microbiol. 2011 Oct 18;2:211</RefSource><PMID Version="1">22022322</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>BMC Bioinformatics. 2010 Mar 08;11:119</RefSource><PMID Version="1">20211023</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nucleic Acids Res. 2014 Jan;42(Database issue):D222-30</RefSource><PMID Version="1">24288371</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Commun. 2013;4:2856</RefSource><PMID Version="1">24292151</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Bacteriol Rev. 1972 Dec;36(4):407-77</RefSource><PMID Version="1">4568761</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 2009 Dec;191(24):7430-5</RefSource><PMID Version="1">19820100</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEMS Microbiol Rev. 2008 Mar;32(2):208-33</RefSource><PMID Version="1">18081839</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Arch Microbiol. 2012 Jun;194(6):505-12</RefSource><PMID Version="1">22231476</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1996 Feb;178(3):906-10</RefSource><PMID Version="1">8550531</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS Comput Biol. 2011 Oct;7(10):e1002195</RefSource><PMID Version="1">22039361</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEMS Microbiol Rev. 2008 Mar;32(2):149-67</RefSource><PMID Version="1">18194336</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1995 Jul;177(14):4121-30</RefSource><PMID Version="1">7608087</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Curr Opin Biotechnol. 2006 Jun;17(3):241-9</RefSource><PMID Version="1">16704931</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEMS Microbiol Rev. 2008 Mar;32(2):168-207</RefSource><PMID Version="1">18266853</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1972 Nov;112(2):950-8</RefSource><PMID Version="1">4563986</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochem Biophys Res Commun. 1969 Aug 15;36(4):682-9</RefSource><PMID Version="1">4897411</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Genet Res. 1972 Aug;20(1):65-74</RefSource><PMID Version="1">4563578</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Eur J Biochem. 1995 May 15;230(1):80-7</RefSource><PMID Version="1">7601127</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Anal Biochem. 1976 May 7;72:248-54</RefSource><PMID Version="1">942051</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Biol Evol. 2015 Jan;32(1):268-74</RefSource><PMID Version="1">25371430</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2013 Jun 13;8(6):e66458</RefSource><PMID Version="1">23785498</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1998 Sep;180(18):4799-803</RefSource><PMID Version="1">9733680</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Protein Expr Purif. 1995 Dec;6(6):757-62</RefSource><PMID Version="1">8746627</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1992 Sep;174(17):5748-52</RefSource><PMID Version="1">1512209</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1992 Mar;174(5):1690-3</RefSource><PMID Version="1">1311302</PMID></CommentsCorrections></CommentsCorrectionsList><OtherID Source="NLM">PMC4803751</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">MurB</Keyword><Keyword MajorTopicYN="N">MurC</Keyword><Keyword MajorTopicYN="N">UDP-N-acetylenolpyruvoylglucosamine reductase</Keyword><Keyword MajorTopicYN="N">UDP-N-acetylmuramate:l-alanine ligase</Keyword><Keyword MajorTopicYN="N">Verrucomicrobium spinosum</Keyword><Keyword MajorTopicYN="N">bacterial cell wall</Keyword><Keyword MajorTopicYN="N">fusion enzyme</Keyword><Keyword MajorTopicYN="N">peptidoglycan</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>01</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>03</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27047475</ArticleId><ArticleId IdType="doi">10.3389/fmicb.2016.00362</ArticleId><ArticleId IdType="pmc">PMC4803751</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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