Dec 1, 1975

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

Journal of Bacteriology
A M AllamT A Elzainy

Abstract

2-Keto-3-deoxygluconate aldolase of Aspergillus 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 Km 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.

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Mentioned in this Paper

Mercury
Aldehyde-Lyases
Pyruvate Measurement
Isocyanides
Cytokinesis of the Fertilized Ovum
Sulfhydryl Compounds
Metals
Glyceraldehyde
Pyruvate
2-keto-3-deoxygluconate aldolase

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