효모 미토콘드리아의 $K^+$-활성화 ALDH을 정제하고 $Li^+$와 $Mg^{2+}$의 영향을 조사한 결과 금속이온의 농도가 50mM일 때 ALDH의 dehydrogenase 활성은 각각 50%, 76% 감소하였으나, esterase 활성은 각각 13%，8%씩 오히려 증가하였다. 이와 같은 실험결과는 $Li^+$와 $Mg^{2+}$가 deacylation을 촉진하는 반면 E-ALDH 복합체로부터의 NADH 분리를 억제하는 것으로 해석되고, $K^+$이 주로 E-NADH 복합체로부터의 NADH 해리반응에 관여함을 뜻하며 E-NADH 복합체로 부터의 NADH의 해리 단계가 효모 미토콘드리아 ALDH 반응의 속도제한 단계일 가능성이 큰 것으로 생각된다.
Yeast (Saccharomyces cerevisiae) mitochondrial $K^+$ activated aldehyde dehydrogenase (ALDH) was purified and the effect of $Li^+$ and $Mg^{2+}$ was investigated. It was found that both 50mM $Li^+$ and $Mg^{2+}$ inhibited the dehydrogenase reaction of ALDH as much as 50% and 76% respectively while the esterase reaction of this enzyme was stimulated 13% and 8%. This suggested that $Li^+$ and $Mg^{2+}$ stimulated deacylation of the intermediate thioester but inhibited the dissociation of Enzyme-NADH complex and the $K^+$ activation might be involved in the dissociation of Enzyme-NADH complex which seemed to be the rate limiting step in the ALDH catalyzed reaction.
