Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136T
Identifieur interne : 001D30 ( Main/Merge ); précédent : 001D29; suivant : 001D31Identification and Partial Characterization of a Novel UDP-N-Acetylenolpyruvoylglucosamine Reductase/UDP-N-Acetylmuramate:l-Alanine Ligase Fusion Enzyme from Verrucomicrobium spinosum DSM 4136T
Auteurs : Kubra F. Naqvi [États-Unis] ; Delphine Patin [France] ; Matthew S. Wheatley [États-Unis] ; Michael A. Savka [États-Unis] ; Renwick C. J. Dobson [Nouvelle-Zélande, 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
Url:
DOI: 10.3389/fmicb.2016.00362
PubMed: 27047475
PubMed Central: 4803751
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PMC:4803751Le document en format XML
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-Acetylenolpyruvoylglucosamine Reductase/UDP-<italic>N</italic>
-Acetylmuramate:<sc>l</sc>
-Alanine Ligase Fusion Enzyme from <italic>Verrucomicrobium spinosum</italic>
DSM 4136<sup>T</sup>
</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification and Partial Characterization of a Novel UDP-<italic>N</italic>
-Acetylenolpyruvoylglucosamine Reductase/UDP-<italic>N</italic>
-Acetylmuramate:<sc>l</sc>
-Alanine Ligase Fusion Enzyme from <italic>Verrucomicrobium spinosum</italic>
DSM 4136<sup>T</sup>
</title>
<author><name sortKey="Naqvi, Kubra F" sort="Naqvi, Kubra F" uniqKey="Naqvi K" first="Kubra F." last="Naqvi">Kubra F. Naqvi</name>
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<country>Rochester, NY, USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
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<author><name sortKey="Patin, Delphine" sort="Patin, Delphine" uniqKey="Patin D" first="Delphine" last="Patin">Delphine Patin</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay</institution>
<country>Orsay, France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
</author>
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<country>Rochester, NY, USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
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<author><name sortKey="Savka, Michael A" sort="Savka, Michael A" uniqKey="Savka M" first="Michael A." last="Savka">Michael A. Savka</name>
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<country>Rochester, NY, USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff3"><institution>Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury</institution>
<country>Christchurch, New Zealand</country>
</nlm:aff>
<country xml:lang="fr">Nouvelle-Zélande</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
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<country>Parkville, VIC, Australia</country>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff5"><institution>Monash University Malaysia Genomics Facility, Monash University Malaysia</institution>
<country>Selangor, Malaysia</country>
</nlm:aff>
<country xml:lang="fr">Malaisie</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff6"><institution>School of Science, Monash University Malaysia</institution>
<country>Selangor, Malaysia</country>
</nlm:aff>
<country xml:lang="fr">Malaisie</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff2"><institution>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay</institution>
<country>Orsay, France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff2"><institution>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay</institution>
<country>Orsay, France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff2"><institution>Institute for Integrative Biology of the Cell, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay</institution>
<country>Orsay, France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</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:aff id="aff1"><institution>Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology</institution>
<country>Rochester, NY, USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>, Santa Cruz</wicri:regionArea>
<wicri:noRegion>Santa Cruz</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j">Frontiers in Microbiology</title>
<idno type="eISSN">1664-302X</idno>
<imprint><date when="2016">2016</date>
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<front><div type="abstract" xml:lang="en"><p>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 <italic>Verrucomicrobium spinosum</italic>
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-<italic>N</italic>
-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-<italic>N</italic>
-acetylmuramate:<sc>l</sc>
-alanine ligase (MurC) that are involved in the cytoplasmic steps of peptidoglycan biosynthesis, was cloned. <italic>In vivo</italic>
analyses using functional complementation showed that the fusion gene was able to complement <italic>Escherichia coli murB</italic>
and <italic>murC</italic>
temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/C<sub><italic>Vs</italic>
</sub>
) was shown to be endowed with UDP-<italic>N</italic>
-acetylmuramate:<sc>l</sc>
-alanine ligase activity. <italic>In vitro</italic>
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 <italic>K</italic>
<sub><italic>m</italic>
</sub>
values for ATP, UDP-MurNAc, and <sc>l</sc>
-alanine were 470, 90, and 25 μM, respectively. However, all attempts to demonstrate an <italic>in vitro</italic>
UDP-<italic>N</italic>
-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.</p>
</div>
</front>
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