来自星杆藻的丙二酸半醛氧化脱羧酶的纯化及性质
The purification and properties of malonic semialdehyde oxidative decarboxylase from Prototheca zopfii.
作者信息
Lloyd D
出版信息
Biochem J. 1965 Sep;96(3):766-70. doi: 10.1042/bj0960766.
Abstract
- An enzyme, which in the presence of NAD(+) and CoA oxidizes malonic semialdehyde to acetyl-CoA, has been purified from an extract of the colourless alga Prototheca zopfii. 2. The purified enzyme has optimum pH7.5, is specific for NAD(+) and requires a thiol compound for maximum activity. 3. The enzyme is inhibited by arsenite, N-ethylmaleimide and urea. 4. The results are discussed in relation to those obtained by other workers with a similar bacterial enzyme, and a possible reaction sequence is proposed.
摘要
- 从无色藻类原藻提取物中纯化出一种酶，该酶在NAD(+)和辅酶A存在的情况下，将丙二酸半醛氧化为乙酰辅酶A。2. 纯化后的酶最适pH值为7.5，对NAD(+)具有特异性，且需要硫醇化合物才能达到最大活性。3. 该酶受到亚砷酸盐、N-乙基马来酰亚胺和尿素的抑制。4. 结合其他研究人员对类似细菌酶的研究结果对这些结果进行了讨论，并提出了可能的反应序列。
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本文引用的文献
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ON THE SITES OF ATTACHMENT AND REACTION OF ALDEHYDE DEHYDROGEN ASES.论醛脱氢酶的附着位点及反应
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Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A.醛氧化。V. 丙二酸半醛直接转化为乙酰辅酶A。
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Arsenite inhibition; a property common to aldehyde dehydrogenases.亚砷酸盐抑制作用；醛脱氢酶的共同特性。
Arch Biochem Biophys. 1957 Aug;70(2):625-7. doi: 10.1016/0003-9861(57)90153-4.
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