EC Number   |
Natural Substrates |
|---|
   3.5.1.104 | acetylated peptidoglycan + H2O |
- |
| 3.5.1.104 | acetylated peptidoglycan + H2O |
enzymatic deacetylation of chemically acetylated vegetative peptidoglycan from Bacillus cereus by BC1960 and BC3618 results in increased resistance to lysozyme digestion |
| 3.5.1.104 | acetylated peptidoglycan + H2O |
enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis |
| 3.5.1.104 | acetylated peptidoglycan + H2O |
N-deacetylation is a major modification of Listeria peptidoglycan. PG N-deacetylation could be a general mechanism used by bacteria to evade the host innate immune system |
| 3.5.1.104 | acetylated peptidoglycan + H2O |
peptidoglycan GlcNAc deacetylase protects the Gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan GlcNAc residues |
| 3.5.1.104 | more |
PdaC acts as a GlcNAc deacetylase toward chitin oligomers and as a MurNAc deacetylase toward Bacillus subtilis peptidoglycan, activity toward MurNAc is higher than toward GlcNAc |
| 3.5.1.104 | peptidoglycan-N-acetyl-D-glucosamine + H2O |
- |
| 3.5.1.104 | peptidoglycan-N-acetyl-D-glucosamine + H2O |
Helicobacter pylori is highly resistant to lysozyme (up to 50 mg/ml), but the HP310 mutant is less resistant compared with the parent strain. The peptidoglycan deacetylation appears to confer lysozyme resistance to escape immunedetection |
| 3.5.1.104 | peptidoglycan-N-acetyl-D-glucosamine + H2O |
peptidoglycan N-deacetylation is an important modification of Listeria peptidoglycan, which allows this human pathogen to evade the innate immune system |
| 3.5.1.104 | peptidoglycan-N-acetyl-D-glucosamine + H2O |
the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria |
