English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We report here the cloning and characterization of a cytoplasmic kinase of Clostridium acetobutylicum , named MurK (for mur ein sugar k inase). 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 m  values of 190 and 127 μM for MurNAc and GlcNAc, respectively, and a k  cat value (65.0 s −1 ) 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.

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