Purification and properties of pyridine nucleotide-independent L-lactate dehydrogenase from Polyporus circinatus.
Cell extracts of Polyporus circinatus grown on lactate catalyze the reduction of 2,6-dichlorophenolindophenol by l-lactate without the participation of nicotinamide adenine dinucleotide or nicotinamide adenine dinucleotide phosphate. The enzyme has been purified 78-fold and was homogenous by disc gel electrophoresis. The optimal pH was found to be 6.7. The Michaelis constant for l-lactate was 5.9 x 10(-4) M and the oxalate inhibition constant was 1.5 x 10(-4) M. The nature of the prosthetic group is discussed.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D001487:Basidiomycota / Q000201:enzymology* / Q000378:metabolism; D002474:Cell-Free System; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D006843:Hydrocarbons, Chlorinated / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007215:Indophenol / Q000378:metabolism; D007773:Lactates / Q000378:metabolism; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D011773:Pyruvates / Q000096:biosynthesis; D013237:Stereoisomerism
D006843:Hydrocarbons, Chlorinated; D007773:Lactates; D011773:Pyruvates; D009243:NAD; D007215:Indophenol; D009249:NADP; D000429:Alcohol Oxidoreductases