3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	-	-	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	catalytic mechanism and substrate binding structure, overview	709012	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	catalytic mechanism, 2 stable states in the double displacement mechanism with formation of a transient covalent arabinofuranosyl-enzyme intermediate, structure of enzyme-substrate complex, substrate binding and specificity	-, 655337	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	catalytic mechanism, Glu175 is the acid-base residue, Glu294 functions as the catalytic nucleophile	-, 656094	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	endolytic mode of action	-, 655155	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	enzyme shows 2 catalytic activities: alpha-L-arabinofuranosidase and beta-D-xylosidase activity	656191	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	exo-acting enzyme	-, 654273	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	mode of action of Penicillium funiculosum family 62 isozymes, overview	731728	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	reaction mechanism, active site structure, Glu28, the catalytic nucleophil, Glu176, the acid-base residue, and Glu298, responsible for modulation of the ionization state of the acid-base and for substrate fixation, are important for catalytic activity	657222	
3.2.1.55	1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose	the enzyme also acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans, some beta-galactosidases, EC 3.2.1.23, and beta-D-fucosidases, EC 3.2.1.38, also hydrolyse alpha-L-arabinosides	-, 654099