Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria.
The malolactic enzyme of Lactobacillus plantarum was purified from 5.5 units/mg to a specific activity of 265 units/mg of protein. The enzyme has an isoelectric point of pH 4.4. The molecular weight is Mr = 140,000 as determined by gradient gel electrophoresis. The enzyme consists of two probably identical subunits (Mr = 70,000) that were observed after treatment with sodium dodecyl sulfate. Malolactic enzyme catalyzes the NAD- and manganese-dependent reaction L-malate leads to CO2 + L-lactate. Therefore, this enzyme can be distinguished from the well known malic enzymes (L-malate: NAD+ oxidoreductase, oxalacetate-decarboxylating EC 1.1.1.38 or 1.1.1.39). Malolactic enzyme is found in most lactic acid bacteria (Lactobacteriaceae); it has not been detected in other bacteria.
D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007773:Lactates / Q000378:metabolism; D019344:Lactic Acid; D007778:Lactobacillus / Q000201:enzymology*; D008291:Malate Dehydrogenase / Q000302:isolation & purification*; D008293:Malates / Q000378:metabolism; D008345:Manganese / Q000378:metabolism; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism
D007773:Lactates; D008293:Malates; D009243:NAD; D019344:Lactic Acid; D008345:Manganese; C030298:malic acid; C037731:malolactic enzyme; D008291:Malate Dehydrogenase