3.2.1.25 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol - 5366 3.2.1.25 (5S,6R,8R)-5-(hydroxymethyl)-2-(2-phenylethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol persuasive transition state mimic 66573 3.2.1.25 (5S,6R,8R)-5-(hydroxymethyl)-2-(phenoxymethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol persuasive transition state mimic 72817 3.2.1.25 (5S,6R,8R)-5-(hydroxymethyl)-2-[(phenylamino)methyl]-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol persuasive transition state mimic 72818 3.2.1.25 2-amino-2-deoxy-D-mannose - 15479 3.2.1.25 2-amino-2-deoxy-D-mannose competitive 15479 3.2.1.25 2-deoxy-2-fluoro-beta-D-mannosyl fluoride time-dependent inactivation through accumulation of a covalent 2-deoxy-2-fluoro-alpha-D-mannosyl-beta-mannosidase 2A enzyme intermediate 55972 3.2.1.25 2-deoxy-2-fluoro-beta-glycosyl fluorides in vivo inhibition 102137 3.2.1.25 4-nitrophenyl beta-D-thioglucoside competitive, adopts 4NP-S-Glc 3S5 or 1S3 conformations upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thioglucoside preferentially binds in 1S3 geometries 85280 3.2.1.25 4-nitrophenyl beta-D-thiomannoside competitive, adopts 4C1 geometry upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thiomannoside preferentially binds in 1S3 geometries 85281 3.2.1.25 Ag+ - 75 3.2.1.25 Ag+ AgNO3 75 3.2.1.25 Ag+ 2 mM, complete inhibition 75 3.2.1.25 Ag+ 1.5 mM, no residual activity 75 3.2.1.25 Ag+ 1 mM, 98% loss of activity 75 3.2.1.25 beta-1,4-mannooligosaccharides inhibit binding of the enzyme to galactomannans 102528 3.2.1.25 Ca2+ 5 mM Ca(NO3)2, 45% inhibition 15 3.2.1.25 Cd2+ - 52 3.2.1.25 Cd2+ CdCl2 52 3.2.1.25 Co2+ 1.5 mM, 80% residual activity 23 3.2.1.25 Co2+ 1 mM, 12% loss of activity 23 3.2.1.25 Cu2+ 0.2 mM, 76% inhibition 19 3.2.1.25 Cu2+ - 19 3.2.1.25 Cu2+ 1.5 mM, no residual activity 19 3.2.1.25 Cu2+ 1 mM, 72% loss of activity 19 3.2.1.25 D-mannono-1,4-lactone - 11057 3.2.1.25 D-mannosamine - 5145 3.2.1.25 D-mannose 10 mM 216 3.2.1.25 D-mannose with p-nitrophenyl-beta-D-mannopyranoside as substrate 216 3.2.1.25 D-mannose - 216 3.2.1.25 D-mannose hydrolysis of p-nitrophenyl beta-D-mannoside, competitive 216 3.2.1.25 dimethyl sulfoxide 5 mM, no residual activity 1217 3.2.1.25 dimethylformamide 5 mM, no residual activity 3631 3.2.1.25 ethanol 5 mM, no residual activity 69 3.2.1.25 Fe3+ - 70 3.2.1.25 guanidine hydrochloride 0.6 M, 30% inhibition 1048 3.2.1.25 Hg2+ - 33 3.2.1.25 Hg2+ HgCl2 33 3.2.1.25 Hg2+ 0.05 mM, 50% inhibition 33 3.2.1.25 Hg2+ 1 mM, 98% loss of activity 33 3.2.1.25 iodoacetate 5 mM, no residual activity 93 3.2.1.25 isofagomine lactam - 129740 3.2.1.25 isoquinuclidine - 151334 3.2.1.25 mannose relative inhibition of 20%, three concentrations of 10, 50, and 100 mM tested 988 3.2.1.25 Mg2+ 1 mM, 4% loss of activity 6 3.2.1.25 Mn2+ 1 mM, 4% loss of activity 11 3.2.1.25 monoiodoacetate - 1473 3.2.1.25 N,N-(2-aminoethyl)-D-glucoamidine - 58956 3.2.1.25 N,N-(2-aminoethyl)-D-mannoamidine - 58961 3.2.1.25 N,N-(3-aminopropyl)-D-glucoamidine - 58957 3.2.1.25 N,N-(3-aminopropyl)-D-mannoamidine - 58962 3.2.1.25 N,N-(3-hydroxypropyl)-D-glucoamidine - 58959 3.2.1.25 N,N-(3-hydroxypropyl)-D-mannoamidine - 58964 3.2.1.25 N,N-(4-aminobutyl)-D-glucoamidine - 58958 3.2.1.25 N,N-(4-aminobutyl)-D-mannoamidine - 58963 3.2.1.25 N,N-propyl-D-mannoamidine - 58960 3.2.1.25 N-bromosuccinimide - 208 3.2.1.25 n-Dodecylbenzene sulfonate - 98112 3.2.1.25 N-propyl-D-glucoamidine - 58955 3.2.1.25 N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]ethane-1,2-diaminium - 73705 3.2.1.25 N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]propan-1-aminium - 73706 3.2.1.25 noeuromycin - 11797 3.2.1.25 p-nitrophenyl-alpha-D-mannopyranoside activates at low concentration, competitively inhibits at higher concentrations, 2-3 mM 1562 3.2.1.25 p-nitrophenyl-alpha-D-mannopyranoside hydrolysis of p-nitrophenyl-beta-D-mannoside 1562 3.2.1.25 p-nitrophenyl-beta-mannoside above 0.4 mM 55973 3.2.1.25 Pb2+ - 139 3.2.1.25 Pb2+ 1.5 mM, 78% residual activity 139 3.2.1.25 PCMB - 78 3.2.1.25 PHMB - 7422 3.2.1.25 PMSF - 248 3.2.1.25 SDS - 124 3.2.1.25 Sodium dodecyl sulfate 5 mM, no residual activity 1358 3.2.1.25 Zn2+ 0.1 mM, 35% inhibition 14 3.2.1.25 Zn2+ - 14 3.2.1.25 Zn2+ 10 mM ZnSO4, 30% inhibition 14 3.2.1.25 Zn2+ 1.5 mM, no residual activity 14