Kasprzak A A, Kochman M
Biochim Biophys Acta. 1980 Apr 11;612(2):455-9. doi: 10.1016/0005-2744(80)90128-x.
A direct interaction of rabbit muscle fructose-1,6-bisphosphate aldolase with NAD+, NADH, and NAD-agarose was demonstrated. The electrostatic forces are primary involved in this interaction. Two specific binding sites for the dinucleotide were observed. One of them is located at the active site of the enzyme, the second is in a region of weak binding site for ATP and fructose 1,6-bisphosphate.
已证实兔肌肉果糖-1,6-二磷酸醛缩酶与NAD⁺、NADH和NAD-琼脂糖存在直接相互作用。静电力主要参与这种相互作用。观察到二核苷酸有两个特异性结合位点。其中一个位于酶的活性位点,另一个在ATP和果糖1,6-二磷酸的弱结合位点区域。