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Literature summary for 3.5.1.104 extracted from

  • Bhattacharjee, N.; Feliks, M.; Shaik, M.M.; Field, M.J.
    Catalytic mechanism of peptidoglycan deacetylase a computational study (2017), J. Phys. Chem. B, 121, 89-99 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of Zn-bound enzyme Helicobacter pylori

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc metalloenzyme, active site-bound Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
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-
-

Synonyms

Synonyms Comment Organism
peptidoglycan deacetylase
-
Helicobacter pylori

General Information

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