Formation and cleavage of 2 keto 3 deoxygluconate by 2 keto 3 deoxygluconate aldolase of Aspergillus niger

Abstract

2 Keto 3 deoxygluconate aldolase of A. niger, an enzyme that has not been reported previously, was purified 468 fold. Maximal activity was obtained at pH 8.0 and 50 C. The enzyme exhibited relative stereochemical specificity with respect to glyceraldehyde. The K(m) values for 2 keto 3 deoxygluconate, glyceraldehyde, and pyruvate were 10, 13.3, and 3.0 mM, respectively. The effects of some compounds and inhibitors on enzyme activity were examined. Stability of the enzyme under different conditions was investigated. The equilibrium constant was about 0.33 x 10-3 M.