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Characterization of a Glucosamine/Glucosaminide N-Acetyltransferase of Clostridium acetobutylicum

Characterization of a Glucosamine/Glucosaminide N-Acetyltransferase of Clostridium acetobutylicum

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REITH, Jan, Christoph MAYER, 2011. Characterization of a Glucosamine/Glucosaminide N-Acetyltransferase of Clostridium acetobutylicum. In: Journal of Bacteriology. American Society for Microbiology (ASM). 193(19), pp. 5393-5399. ISSN 0021-9193. eISSN 1098-5530. Available under: doi: 10.1128/JB.05519-11

@article{Reith2011-10Chara-51138, title={Characterization of a Glucosamine/Glucosaminide N-Acetyltransferase of Clostridium acetobutylicum}, year={2011}, doi={10.1128/JB.05519-11}, number={19}, volume={193}, issn={0021-9193}, journal={Journal of Bacteriology}, pages={5393--5399}, author={Reith, Jan and Mayer, Christoph} }

2020-09-30T09:35:00Z Mayer, Christoph Mayer, Christoph 2020-09-30T09:35:00Z Reith, Jan Characterization of a Glucosamine/Glucosaminide N-Acetyltransferase of Clostridium acetobutylicum Many bacteria, in particular Gram-positive bacteria, contain high proportions of non-N-acetylated amino sugars, i.e., glucosamine (GlcN) and/or muramic acid, in the peptidoglycan of their cell wall, thereby acquiring resistance to lysozyme. However, muramidases with specificity for non-N-acetylated peptidoglycan have been characterized as part of autolytic systems such as of Clostridium acetobutylicum. We aim to elucidate the recovery pathway for non-N-acetylated peptidoglycan fragments and present here the identification and characterization of an acetyltransferase of novel specificity from C. acetobutylicum, named GlmA (for glucosamine/glucosaminide N-acetyltransferase). The enzyme catalyzes the specific transfer of an acetyl group from acetyl coenzyme A to the primary amino group of GlcN, thereby generating N-acetylglucosamine. GlmA is also able to N-acetylate GlcN residues at the nonreducing end of glycosides such as (partially) non-N-acetylated peptidoglycan fragments and β-1,4-glycosidically linked chitosan oligomers. K<sub>m</sub> values of 114, 64, and 39 μM were determined for GlcN, (GlcN)<sub>2</sub>, and (GlcN)<sub>3</sub>, respectively, and a 3- to 4-fold higher catalytic efficiency was determined for the di- and trisaccharides. GlmA is the first cloned and biochemically characterized glucosamine/glucosaminide N-acetyltransferase and a member of the large GCN5-related N-acetyltransferases (GNAT) superfamily of acetyltransferases. We suggest that GlmA is required for the recovery of non-N-acetylated muropeptides during cell wall rescue in C. acetobutylicum. Reith, Jan 2011-10 eng

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