no activity on branched alpha-mannan, alpha-1,6-mannans that contain side chains, little or no activity with glucans: amylose, dextran, cellulose, laminarin, alpha-1,6-mannobiose, reduced mannobiose, reduced mannotriose, no activity with methyl alpha-D-mannoside or p-nitrophenyl alpha-D-mannoside, no activity with beta-1,4-D-mannan, methyl alpha-D-mannopyranoside or p-nitrophenyl alpha-D-mannopyranoside
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the non-hydrolyzable S-linked azasugars, 1,6-alpa-mannosylthio- and 1,6-alpha-mannobiosylthioisofagomine bind with high affinity to the enzyme. X-ray crystallography shows an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener