PMID: 358Dec 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.

Citations

Jan 29, 2005·Journal of Basic Microbiology·A M. ElshafeiLatifa A Mohamed
Jun 28, 2007·Letters in Applied Microbiology·G FeronC Blin-Perrin
Jan 1, 1995·Antonie van Leeuwenhoek·A M. ElshafeiO M. Abdel-Fatah
Jan 18, 2019·International Journal of Molecular Sciences·Weijie ZhaiZhijun Liu

Related Concepts

Aldehyde-Lyases
Aspergillus
Aspergillus niger
Isocyanides
Drug Stability
Edetic Acid, Calcium, Sodium Salt
Enzyme Induction
Gluconates
Hydrogen-Ion Concentration
Iodoacetic Acids

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