EC Number |
Reaction |
Reference |
---|
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
- |
- |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
Asp314 is located proximal to the 1''-O-linkage in substrates. Asp314 might protonate the leaving group (general acid), forming an oxocarbenium ion intermediate, and then activate the water (general base) for back-side attack. The W1 ligand of MgB can serve as the nucleophile attacking the anomeric C1'' of the ribose'' |
754165 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
canonical enzyme catalytic mechanism, modelling, overview |
732568 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
catalytic mechanism, modelling, overview |
732351 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
catalytic mechanism, structure-function analysis, overview |
732776 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
enzyme catalytic mechanism, overview |
732714 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes |
-, 754824 |
3.2.1.143 | (ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose |
reaction mechanism and structure, overview |
754168 |