Substrate specificity of PpLGDH
Activities for 20 mm substrate were measured in 2 mm NAD+, 1 mg/ml BSA, and 50 mm Tris-HCl (pH 8.5) at 40 °C. Numbers in parentheses indicate relative activity compared with that of LG (100%). The enzyme showed no significant activity (<0.2% compared with that of LG) toward scyllo-inositol, l-glucose, d-galactosan (1,6-anhydro-β-d-galactopyranose), sedoheptulosan (2,7-anhydro-β-d-altro-heptulopyranose), 1,5-anhydro-d-fructose, d-ribose, d-allose, d-fructose, d-galactose, d-mannose, l-arabinose, l-rhamnose, 1,5-anhydro-d-mannitol, sorbitol (d-glucitol), xylitol, dulcitol (galactitol), erythritol, α-d-glucose 1-phosphate, cellobiose, sucrose, lactose, maltose, and trehalose. NADH-dependent reductase activities (reverse reaction) toward 1,5-anhydro-d-fructose and d-glucono-1,5-lactone were also not detected.