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. 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 IG, Mavromatis K, Deli A, Hayhurst E, Foster SJ, Vårum KM, Bouriotis V (September 2005). "Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis". The Journal of Biological Chemistry. 280 (35): 30856–63. doi:10.1074/jbc.m407426200. PMID 15961396.
Tsalafouta A, Psylinakis E, Kapetaniou EG, Kotsifaki D, Deli A, Roidis A, Bouriotis V, Kokkinidis M (March 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 Crystallographica Section F. 64 (Pt 3): 203–5. doi:10.1107/s1744309108002510. PMC 2374148. PMID 18323609.
Blair DE, Schüttelkopf AW, MacRae JI, van Aalten DM (October 2005). "Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor". Proceedings of the National Academy of Sciences of the United States of America. 102 (43): 15429–34. doi:10.1073/pnas.0504339102. PMC 1252587. PMID 16221761.
Wang G, Olczak A, Forsberg LS, Maier RJ (March 2009). "Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori". The Journal of Biological Chemistry. 284 (11): 6790–800. doi:10.1074/jbc.m808071200. PMC 2652260. PMID 19147492.
Popowska M, Kusio M, Szymanska P, Markiewicz Z (September 2009). "Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis". Journal of Microbiology and Biotechnology. 19 (9): 932–45. doi:10.4014/jmb.0810.557. PMID 19809250.
Fittipaldi N, Sekizaki T, Takamatsu D, de la Cruz Domínguez-Punaro M, Harel J, Bui NK, Vollmer W, Gottschalk M (December 2008). "Significant contribution of the pgdA gene to the virulence of Streptococcus suis". Molecular Microbiology. 70 (5): 1120–35. doi:10.1111/j.1365-2958.2008.06463.x. PMID 18990186.

External links

Peptidoglycan-N-acetylglucosamine+deacetylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.5.1