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