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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.5.1.104
246602
Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls
Biochem. Biophys. Res. Commun.
45
751-758
1971
Bacillus cereus
4256847
3.5.1.104
687462
Enzymic deacetylation of N-acetylglucosamine residues in cell wall peptidoglycan
J. Biochem.
88
469-479
1980
Bacillus cereus
6774970
3.5.1.104
687500
Peptidoglycan N-Acetylglucosamine Deacetylases from Bacillus cereus, Highly Conserved Proteins in Bacillus anthracis
J. Biol. Chem.
280
30856-30863
2005
Bacillus cereus
15961396
3.5.1.104
689736
Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
Proc. Natl. Acad. Sci. USA
102
15429-15434
2005
Streptococcus pneumoniae
16221761
3.5.1.104
689788
A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system
Proc. Natl. Acad. Sci. USA
104
997-1002
2007
Listeria monocytogenes
17215377
3.5.1.104
688863
Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis
Microbiology
153
3275-3285
2007
Lactococcus lactis
17906127
3.5.1.104
688863
Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis
Microbiology
153
3275-3285
2007
Lactococcus lactis IL1403
17906127
3.5.1.104
684195
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
64
203-205
2008
Bacillus cereus
18323609
3.5.1.104
700913
Resistance to mucosal lysozyme compensates for the fitness deficit of peptidoglycan modifications by Streptococcus pneumoniae
PLoS Pathog.
4
e1000241
2008
Streptococcus pneumoniae
19079576
3.5.1.104
700275
Significant contribution of the pgdA gene to the virulence of Streptococcus suis
Mol. Microbiol.
70
1120-1135
2008
Streptococcus suis
18990186
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