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. 2018 Sep 17;293(45):17375–17386. doi: 10.1074/jbc.RA118.004963

Table 1.

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.

Substrate Specific activity
units/mg
LG 17.8 (100)
l-Sorbose 0.73 (4.1)
1,5-Anhydro-d-glucitol 0.65 (3.8)
d-Xylose 0.31 (1.7)
Methyl-α-d-glucopyranoside 0.10 (0.56)
d-Glucose 0.090 (0.50)