Author:
Allam A M,Hassan M M,Elzainy T A
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference11 articles.
1. Occurrence of a modified Entner-Doudoroff pathway in Clostridium aceticum;Andreesen J. R.;Arch. Mikrobiol.,1969
2. D-fucose metabolism in a Pseudomonad. IV. Cleavage of 2- keto-3-deoxy-D-fuconate to pyruvate and D-lactaldehyde by 2-keto-3-deoxy-L-arabonate aldolase;Dahms A. S.;J. Biol. Chem.,1972
3. Nonphosphorylated system for gluconate catabolism in fungi;Elzainy T. A.;Egypt. J. Chem.,1971
4. Physiological studies on gluconate utilization by Aspergillus niger;Elzainy T. A.;Egypt. J. Bot.,1972
5. New pathwav for nonphosphorylated degradation of gluconate by Aspergillus niger;Elzainy T. A.;J. Bacteriol.,1973
Cited by
15 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献