Journal article
Identification and partial characterization of a novel UDP-N-acetylenolpyruvoylglucosamine reductase/UDP-N-acetylmuramate: L-alanine ligase fusion enzyme from Verrucomicrobium spinosum DSM 4136T
KF Naqvi, D Patin, MS Wheatley, MA Savka, RCJ Dobson, HM Gan, H Barreteau, D Blanot, D Mengin-Lecreulx, AO Hudson
Frontiers in Microbiology | Published : 2016
Open access
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 i..
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Awarded by Army Research Laboratory
Funding Acknowledgements
All, KN, MW, and MS thank the Thomas H. Gosnell School of Life Sciences (GSOLS) and the College of Science (COS) at the Rochester Institute of Technology (RIT) for ongoing support. This work was supported by a Dean's Research Initiation (D-RIG) awarded to AH by the COS at RIT. HG acknowledges the support from the i'Vlonash University Malaysia Tropical Medicine and Biology Multidisciplinary Platform. RD acknowledges the following for funding support in part: (1) the Ministry of Business, Innovation, and Employment (contract UOCX1208), (2) the New Zealand Royal Society Marsden Fund (contract UOC1013), and (3) the US Army Research Laboratory and US Army Research Office under contract/grant number W911NF-11-1-0481. This work was also supported by grants from the Centre National de la Recherche Scientifique (UMR 9198).