Crystallization (Comment) | Organism |
---|---|
crystal structure analysis of Zn-bound enzyme | Helicobacter pylori |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc metalloenzyme, active site-bound | Helicobacter pylori |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Helicobacter pylori | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
peptidoglycan deacetylase | - |
Helicobacter pylori |
General Information | Comment | Organism |
---|---|---|
additional information | catalytic mechanism possibilities analyzed using the mechanism of reaction of acetyl removal from a model substrate, the N-acetylglucosamine/N-acetylmuramic acid dimer by peptidogylcan deacetylase. Analysis via hybrid quantum chemical/molecular mechanical potential calculations (QC/MM), in conjunction with reaction-path-finding algorithms, molecular docking and molecular dynamics simulations, overview. The active site of this enzyme is in a region of highly negative electrostatic potential and contains a zinc dication with a bound water molecule | Helicobacter pylori |