Peptidoglycan-N-acetylglucosamine deacetylase

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

\rightleftharpoons

peptidoglycan-D-glucosamine + acetate

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

References

↑ Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and 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.
↑ Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and 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.
↑ Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and 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.
↑ Wang, G., Olczak, A., Forsberg, L.S. and 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.
↑ Popowska, M., Kusio, M., Szymanska, P. and 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.
↑ Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and 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.

External links

Peptidoglycan-N-acetylglucosamine deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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