Peptidoglycan-N-acetylglucosamine deacetylase

Peptidoglycan-N-acetylglucosamine deacetylase
Identifiers
EC number 3.5.1.104
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N-acetylglucosamine amidohydrolase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

peptidoglycan-N-acetyl-D-glucosamine + H2O peptidoglycan-D-glucosamine + acetate

This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.

References

  1. Psylinakis, E.; Boneca, I.G.; Mavromatis, K.; Deli, A.; Hayhurst, E.; Foster, S.J.; Varum, K.M.; Bouriotis, V. (2005). "Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis". J. Biol. Chem. 280: 30856–30863. doi:10.1074/jbc.m407426200. PMID 15961396.
  2. Tsalafouta, A.; Psylinakis, E.; Kapetaniou, E.G.; Kotsifaki, D.; Deli, A.; Roidis, A.; Bouriotis, V.; Kokkinidis, M. (2008). "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: 203–205. doi:10.1107/s1744309108002510. PMID 18323609.
  3. Blair, D.E.; Schuttelkopf, A.W.; MacRae, J.I.; van Aalten, D.M. (2005). "Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor". Proc. Natl. Acad. Sci. USA. 102: 15429–15434. doi:10.1073/pnas.0504339102. PMID 16221761.
  4. Wang, G.; Olczak, A.; Forsberg, L.S.; Maier, R.J. (2009). "Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori". J. Biol. Chem. 284: 6790–6800. doi:10.1074/jbc.m808071200. PMID 19147492.
  5. Popowska, M.; Kusio, M.; Szymanska, P.; Markiewicz, Z. (2009). "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: 932–945. doi:10.4014/jmb.0810.557. PMID 19809250.
  6. Fittipaldi, N.; Sekizaki, T.; Takamatsu, D.; de la Cruz Domínguez-Punaro, M.; Harel, J.; Bui, N.K.; Vollmer, W.; Gottschalk, M. (2008). "Significant contribution of the pgdA gene to the virulence of Streptococcus suis". Mol. Microbiol. 70: 1120–1135. doi:10.1111/j.1365-2958.2008.06463.x. PMID 18990186.
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