Lipoyl dehydrogenase from Saccharomyces cerevisiae II. Kinetic and inhibitor studies

A. Wren , V. Massey
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引用次数: 10

Abstract

Kinetic and inhibitor studies have been carried out on lipoyl dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) from Saccharomyces cerevisiae. The results obtained are similar in many respects to those reported for the enzyme prepared from pig heart although some differences have been observed. The overall picture of activity with various electron donors and acceptors is qualitively the same with the two enzymes, the yeast enzyme showing considerably greater activity using K3Fe(CN)6 and oxidized 3-acetylpyridine-adenine dinucleotide as electron acceptors. Inhibition of the enzyme by arsenite and copper ions is less marked than that of pig-heart lipoyl dehydrogenase, though again the results are qualitively very similar.

酿酒酵母菌的脂酰脱氢酶。动力学和抑制剂研究
对酿酒酵母脂酰脱氢酶(NADH:lipoamide oxidoreductase, EC 1.6.4.3)的动力学和抑制剂进行了研究。所得结果在许多方面与报道的从猪心脏制备的酶相似,尽管也观察到一些差异。两种酶在不同电子给体和受体作用下的活性总体上是相同的,酵母酶在使用K3Fe(CN)6和氧化3-乙酰吡啶-腺嘌呤二核苷酸作为电子受体时表现出明显更高的活性。亚砷酸盐和铜离子对该酶的抑制作用不如猪心脏脂酰脱氢酶明显,尽管结果在质量上非常相似。
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