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Characterization of an N-Acetylmuramic Acid/N-Acetylglucosamine Kinase of Clostridium acetobutylicum

Characterization of an N-Acetylmuramic Acid/N-Acetylglucosamine Kinase of Clostridium acetobutylicum

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REITH, Jan, Anne BERKING, Christoph MAYER, 2011. Characterization of an N-Acetylmuramic Acid/N-Acetylglucosamine Kinase of Clostridium acetobutylicum. In: Journal of Bacteriology. American Society for Microbiology (ASM). 193(19), pp. 5386-5392. ISSN 0021-9193. eISSN 1098-5530. Available under: doi: 10.1128/JB.05514-11

@article{Reith2011-10Chara-51053, title={Characterization of an N-Acetylmuramic Acid/N-Acetylglucosamine Kinase of Clostridium acetobutylicum}, year={2011}, doi={10.1128/JB.05514-11}, number={19}, volume={193}, issn={0021-9193}, journal={Journal of Bacteriology}, pages={5386--5392}, author={Reith, Jan and Berking, Anne and Mayer, Christoph} }

Berking, Anne Characterization of an N-Acetylmuramic Acid/N-Acetylglucosamine Kinase of Clostridium acetobutylicum eng Berking, Anne Reith, Jan 2020-09-28T09:58:09Z 2020-09-28T09:58:09Z 2011-10 Reith, Jan Mayer, Christoph We report here the cloning and characterization of a cytoplasmic kinase of Clostridium acetobutylicum, named MurK (for murein sugar kinase). The enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), which are phosphorylated at the 6-hydroxyl group. Kinetic analyses revealed K<sub>m</sub> values of 190 and 127 μM for MurNAc and GlcNAc, respectively, and a k<sub>cat</sub> value (65.0 s<sup>−1</sup>) that was 1.5-fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc were substrates for the enzyme. MurK displays low overall amino acid sequence identity (24%) with human GlcNAc kinase and is the first characterized bacterial representative of the BcrAD/BadFG-like ATPase family. We propose a role of MurK in the recovery of muropeptides during cell wall rescue in C. acetobutylicum. The kinase was applied for high-sensitive detection of the amino sugars in cell wall preparations by radioactive phosphorylation. Mayer, Christoph

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