Enolase from spores and cells of Bacillus megaterium: two-step purification of the enzyme and some of its properties.
A simple two-step procedure for purification of enolase from germinated spores or vegetative cells of Bacillus megaterium is described. The procedure resulted in a 1,200-fold purification with production of homogeneous enzyme in approximately 75% yield; the enzymes from spores and cells seemed identical. The molecular weight of the native enzyme was 335,000, with a subunit molecular weight of 42,000. The enzyme required Mg2+ and was inhibited by ethylenediaminetetraacetic acid and fluoride ions. The Michaelis constants for 2-phosphoglyceric acid and Mg2+ were 7.1 X 10(-4) and 4.7 X 10(-4) M, respectively.
D001410:Bacillus megaterium / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D005459:Fluorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D010751:Phosphopyruvate Hydratase / Q000302:isolation & purification* / Q000378:metabolism; D013171:Spores, Bacterial / Q000201:enzymology
D004492:Edetic Acid; D010751:Phosphopyruvate Hydratase; D008274:Magnesium; D005459:Fluorides