在肌肉和酵母醛缩酶反应中用作底物的D-果糖1,6-二磷酸的异头形式。
The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions.
作者信息
Schray K J, Fishbein R, Bullard W P, Benkovic S J
出版信息
J Biol Chem. 1975 Jul 10;250(13):4883-7.
PMID:168195
Abstract
From a series of rapid quench kinetic experiments, it has been demonstrated that muscle D-fructose bisphosphate aldolase catalyzes the cleavage of beta-D-fructose 1,6-bisphosphate but not that of the alpha anomer, although the alpha anomer may be tightly bound. Yeast D-fructose bisphosphate aldolase appears to utilize both alpha and beta anomers of the substrate, with yeast apoaldolase catalyzing the interconversion of the alpha and beta forms.
摘要
通过一系列快速淬灭动力学实验已证明，肌肉中的D-果糖-1,6-二磷酸醛缩酶催化β-D-果糖-1,6-二磷酸的裂解，但不催化α异头物的裂解，尽管α异头物可能紧密结合。酵母D-果糖-1,6-二磷酸醛缩酶似乎利用底物的α和β两种异头物，酵母脱辅基醛缩酶催化α和β形式的相互转化。
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