Glycerol 3-phosphate Oxidase from Pediococcus sp.

Glycerol 3-phosphate Oxidase from Pediococcus sp. has been used in the kinetic assay to study gluconeogenesis in liver and in immobilization studies on pencil graphite (PG) electrode.

This enzyme is useful for enzymatic determination of triglyceride when coupled with lipoprotein lipase (LPL-311, LPL-314) and glycerokinase (GYK-301, GYK-311) in clinical analysis.

Glycerol 3-phosphate Oxidase is a FAD-dependent α-glycerophosphate oxidase and catalyzes the formation of dihydroxyacetonephosphate. Glycerol 3-phosphate oxidase comprises of a flavin adenine dinucleotide (FAD) and a substrate binding domain and corresponds to molecular weight of 42 kDa. It exists as a monomer and the active site comprises of isoalloxazine ring and histidine 53, arginine 316 and lysine 345 residues crucial for ligand binding.

Isoelectric point : 4.1 -/+0.1
Michaelis constants : 3.2x10 ^-3M (L-α-Glycerophosphate), 6.8 x 10 ^-3M (D, L-form)
Inhibitors : Ionic detergents (SDS, LBS, etc.), Hg⁺⁺, Ag⁺
Optimum pH : 8.0 - 8.5Optimum temperature : 35 - 40o^C
pH Stability : pH 6.5 - 8.5 (25o^C, 20hr) Thermal stability : below 40oC (pH 7.0, 15min)
Substrate specificity : The enzyme has the highest specificity for L-form of a-γlycerophosphate

One unit will oxidize 1.0 μmole of L-glycerol 3-phosphate to dihydroxyacetone phosphate with the formation of H₂O₂ per min at 37°C, at the appropriate pH.

Lyophilized powder containing stabilizers