谷氨酸棒杆菌的NADH脱氢酶。能够氧化NADPH的NADH脱氢酶II同源物的纯化。
NADH dehydrogenase of Corynebacterium glutamicum. Purification of an NADH dehydrogenase II homolog able to oxidize NADPH.
作者信息
Matsushita K, Otofuji A, Iwahashi M, Toyama H, Adachi O
机构信息
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 753-8515, Yamaguchi, Japan.
出版信息
FEMS Microbiol Lett. 2001 Nov 13;204(2):271-6. doi: 10.1111/j.1574-6968.2001.tb10896.x.
NADPH oxidase activity, in addition to NADH oxidase activity, has been shown to be present in the respiratory chain of Corynebacterium glutamicum. In this study, we tried to purify NADPH oxidase and NADH dehydrogenase activities from the membranes of C. glutamicum. Both the enzyme activities were simultaneously purified in the same fraction, and the purified enzyme was shown to be a single polypeptide of 55 kDa. The N-terminal sequence of the enzyme was consistent with the sequence deduced from the NADH dehydrogenase gene of C. glutamicum, which has been sequenced and shown to be a homolog of NADH dehydrogenase II. In addition to high NADH-ubiquinone-1 oxidoreductase activity at neutral pH, the purified enzyme showed relatively high NADPH oxidase and NADPH-ubiquinone-1 oxidoreductase activities at acidic pH. Thus, NADH dehydrogenase of C. glutamicum was shown to be rather unique in having a relatively high reactivity toward NADPH.
除了NADH氧化酶活性外，NADPH氧化酶活性也已被证明存在于谷氨酸棒杆菌的呼吸链中。在本研究中，我们试图从谷氨酸棒杆菌的细胞膜中纯化NADPH氧化酶和NADH脱氢酶活性。两种酶活性在同一组分中同时被纯化，并且纯化后的酶显示为一条55 kDa的单一多肽。该酶的N端序列与从谷氨酸棒杆菌的NADH脱氢酶基因推导的序列一致，该基因已被测序并显示为NADH脱氢酶II的同源物。除了在中性pH下具有高NADH-泛醌-1氧化还原酶活性外，纯化后的酶在酸性pH下还显示出相对较高的NADPH氧化酶和NADPH-泛醌-1氧化还原酶活性。因此，谷氨酸棒杆菌的NADH脱氢酶对NADPH具有相对较高的反应性，这一点相当独特。
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