KEGG   ENZYME: 3.5.1.104Help
Entry
EC 3.5.1.104                Enzyme                                 

Name
peptidoglycan-N-acetylglucosamine deacetylase;
HP310;
PgdA;
SpPgdA;
BC1960;
peptidoglycan deacetylase;
N-acetylglucosamine deacetylase;
peptidoglycan GlcNAc deacetylase;
peptidoglycan N-acetylglucosamine deacetylase;
PG N-deacetylase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
peptidoglycan-N-acetylglucosamine amidohydrolase
Reaction(IUBMB)
peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate [RN:R09721]
Reaction(KEGG)
Substrate
peptidoglycan-N-acetyl-D-glucosamine;
H2O [CPD:C00001]
Product
peptidoglycan-D-glucosamine [CPD:C19842];
acetate [CPD:C00033]
Comment
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].
History
EC 3.5.1.104 created 2010
Reference
1  [PMID:15961396]
  Authors
Psylinakis E, Boneca IG, Mavromatis K, Deli A, Hayhurst E, Foster SJ, Varum KM, Bouriotis V
  Title
Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis.
  Journal
J. Biol. Chem. 280 (2005) 30856-63.
  Organism
Bacillus cereus
Reference
2  [PMID:18323609]
  Authors
Tsalafouta A, Psylinakis E, Kapetaniou EG, Kotsifaki D, Deli A, Roidis A, Bouriotis V, Kokkinidis M
  Title
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.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 64 (2008) 203-5.
  Organism
Bacillus cereus
Reference
3  [PMID:16221761]
  Authors
Blair DE, Schuttelkopf AW, MacRae JI, van Aalten DM
  Title
Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15429-34.
  Organism
Streptococcus pneumoniae
  Sequence
[spr:spr1333]
Reference
4  [PMID:19147492]
  Authors
Wang G, Olczak A, Forsberg LS, Maier RJ
  Title
Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori.
  Journal
J. Biol. Chem. 284 (2009) 6790-800.
  Organism
Helicobacter pylori
Reference
5  [PMID:19809250]
  Authors
Popowska M, Kusio M, Szymanska P, Markiewicz Z
  Title
Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis.
  Journal
J. Microbiol. Biotechnol. 19 (2009) 932-45.
  Organism
Listeria monocytogenes
Reference
6  [PMID:18990186]
  Authors
Fittipaldi N, Sekizaki T, Takamatsu D, de la Cruz Dominguez-Punaro M, Harel J, Bui NK, Vollmer W, Gottschalk M
  Title
Significant contribution of the pgdA gene to the virulence of Streptococcus suis.
  Journal
Mol. Microbiol. 70 (2008) 1120-35.
  Organism
Streptococcus suis
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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