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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >FROM PHOSPHATASES TO VANADIUM PEROXIDASES - A SIMILAR ARCHITECTURE OF THE ACTIVE SITE
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FROM PHOSPHATASES TO VANADIUM PEROXIDASES - A SIMILAR ARCHITECTURE OF THE ACTIVE SITE

机译:从磷酸酶到钒过氧化物酶-活性位点的相似结构

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摘要

We show here that the amino acid residues contributing to the active sites of the vanadate containing haloperoxidases are conserved within three families of acid phosphatases; this suggests that the active sites of these enzymes are very similar, This is confirmed by activity measurements showing that apochloroperoxidase exhibits phosphatase activity, These observations not only reveal interesting evolutionary relationships between these groups of enzymes but may also have important implications for the research on acid phosphatases, especially glucose-6-phosphatase-the enzyme affected in von Gierke disease-of which the predicted membrane topology may have to be reconsidered. [References: 37]
机译:我们在这里表明,贡献于含有卤化过氧化物的钒酸盐的活性位点的氨基酸残基在酸性磷酸酶的三个家族中是保守的。这表明这些酶的活性位点非常相似,这通过活性测量证实,载脂蛋白过氧化物酶具有磷酸酶活性。这些观察结果不仅揭示了这些酶之间有趣的进化关系,而且可能对酸的研究具有重要意义。磷酸酶,尤其是葡萄糖6磷酸酶-冯·吉尔克病中受影响的酶-必须重新考虑其预测的膜拓扑。 [参考:37]

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