[啤酒酵母硫胺素焦磷酸激酶与硫胺素和腺苷-5'-三磷酸的相互作用]
[Interaction of thiamine pyrophosphokinase from brewer's yeast with thiamine and adenosine-5'-triphosphate].
作者信息
Voskoboev A I, Chernikevich I P
出版信息
Biokhimiia. 1977 Jan;42(1):79-84.
PMID:192344
Abstract
The interaction of thiamine pyrophosphokinase (Thiaminkinase EC 2.7.6.2) with thiamine and ATP was studied. It was shown that the mechanism of the thiaminokinase reactions is Rapid Equilibrium Random Bi -- Bi. The enzyme binds 8 moles ATP and 1 mole thiamine per mole protein Ks = 0,8-10(-3) and 4.10(-6) M for ATP and thiamine respectively.
摘要
对硫胺素焦磷酸激酶（硫胺素激酶，EC 2.7.6.2）与硫胺素和ATP的相互作用进行了研究。结果表明，硫胺素激酶反应的机制是快速平衡随机双双反应。该酶每摩尔蛋白质结合8摩尔ATP和1摩尔硫胺素，ATP和硫胺素的Ks分别为0.8×10⁻³和4.1×10⁻⁶M。
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