The Enzyme Database

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Accepted name: peptidoglycan-N-acetylglucosamine deacetylase
Reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate
Other name(s): HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase
Systematic name: peptidoglycan-N-acetylglucosamine amidohydrolase
Comments: Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and Bouriotis, V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J. Biol. Chem. 280 (2005) 30856–30863. [DOI] [PMID: 15961396]
2.  Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and Kokkinidis, M. Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 203–205. [DOI] [PMID: 18323609]
3.  Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and van Aalten, D.M. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. USA 102 (2005) 15429–15434. [DOI] [PMID: 16221761]
4.  Wang, G., Olczak, A., Forsberg, L.S. and Maier, R.J. Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J. Biol. Chem. 284 (2009) 6790–6800. [DOI] [PMID: 19147492]
5.  Popowska, M., Kusio, M., Szymanska, P. and Markiewicz, Z. Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J. Microbiol. Biotechnol. 19 (2009) 932–945. [PMID: 19809250]
6.  Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and Gottschalk, M. Significant contribution of the pgdA gene to the virulence of Streptococcus suis. Mol. Microbiol. 70 (2008) 1120–1135. [DOI] [PMID: 18990186]
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