Voskoboev A I, Chernikevich I P, Ostrovsky Y M
Prikl Biokhim Mikrobiol. 1975 Mar-Apr;11(2):230-6.
Thiamine pyrophosphokinase (EC 2.7.7.2) isolated from dry brewing yeast has been purified 20-fold with a 70% yield. Certain properties of the enzyme have been determined: pH and temperature optima, donor and acceptor concentrations, and relationship between the rate of cocarboxylase biosynthesis and the incubation time and the enzyme quantity. The effects of concentrations of bivalent metal ions Co2+, Mg2+ and Mn2+ on the rate of the enzymic reaction has been studied. A change in the pH optimum as a function of the nature of the ion-activator has been investigated. It has been shown that neopyrithiamin is a competitive inhibitor and oxythiamin inhibits the enzymic reaction insignificantly. Thiamine phosphate cannot be transformed into thiamine diphosphate by the purified enzyme.
从干酿酒酵母中分离出的硫胺素焦磷酸激酶（EC 2.7.7.2）已被纯化20倍，产率为70%。已测定了该酶的某些特性：最适pH值和温度、供体和受体浓度，以及辅羧酶生物合成速率与孵育时间和酶量之间的关系。研究了二价金属离子Co2+、Mg2+和Mn2+的浓度对酶促反应速率的影响。研究了最适pH值随离子激活剂性质的变化。结果表明，新吡硫胺是一种竞争性抑制剂，氧硫胺对酶促反应的抑制作用不明显。纯化后的酶不能将硫胺素磷酸转化为硫胺素二磷酸。
