黑曲霉2-酮-3-脱氧葡萄糖酸醛缩酶催化2-酮-3-脱氧葡萄糖酸的形成与裂解
Formation and cleavage of 2-keto-3-deoxygluconate by 2-keto-3-deoxygluconate aldolase of Aspergillus niger.
作者信息
Allam A M, Hassan M M, Elzainy T A
出版信息
J Bacteriol. 1975 Dec;124(3):1128-31. doi: 10.1128/jb.124.3.1128-1131.1975.
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.
摘要
黑曲霉的2-酮-3-脱氧葡萄糖酸醛缩酶是一种此前未被报道过的酶，已被纯化了468倍。在pH 8.0和50℃时获得最大活性。该酶对甘油醛表现出相对立体化学特异性。2-酮-3-脱氧葡萄糖酸、甘油醛和丙酮酸的米氏常数分别为10、13.3和3.0 mM。研究了一些化合物和抑制剂对酶活性的影响。考察了该酶在不同条件下的稳定性。平衡常数约为0.33×10⁻³ M。
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