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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase
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Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase

机译：功能性旁系同源转移突变的鉴定：大肠杆菌苹果酸脱氢酶向乳酸脱氢酶的转化

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摘要

Five positions in the Escherichia coli malate dehydrogenase (eMDH) sequence, which distinguish MDH from lactate dehydrogenase (LDH) activity, were identified through a combination of Venn diagrams constructed from whole genomic data and from unbiased representative sequences from terminal clades. Incorporation of the five changes in eMDH sufficed to convert the enzyme from one with(K_(cat)/K_m~(pyruvate)/(K_(cat)/K_m/~(oxaloacetate) = 6.1 × 10~(-9) to one with that ratio = 28. The substrate specificity was thus changed by a factor of 4.6 × 10~9. The (K_(cat)/K_m~(pyruvate) value for the pentamutant (eMDH I12V/R81Q/M85E/G210A/V214I) is 3,500 M~(-1)·s~(-1), which is ≈ 1/1,000 of the values found for typical wild-type LDHs. The procedure isolates an intersection of "strong forcing sets" that should prove to be of general use in switching paralog function.
机译：通过从整个基因组数据和末端进化枝的无偏见代表性序列构建的维恩图的组合中，鉴定出了苹果酸苹果酸脱氢酶（eMDH）序列中的五个位置，这些位置将MDH与乳酸脱氢酶（LDH）活性区分开。结合eMDH中的五种变化足以将酶从（K_（cat）/ K_m〜（丙酮酸）/（K_（cat）/ K_m /〜（草酰乙酸）= 6.1×10〜（-9））转化为一种比率为28，因此底物特异性改变了4.6×10〜9。五突变体（eMDH I12V / R81Q / M85E / G210A / V214I）的（K_（cat）/ K_m〜（丙酮酸盐）值为3,500 M〜（-1）·s〜（-1），约为典型野生型LDH值的1 / 1,000，该过程分离出了“强力集”的交集，该交集应证明是一般用于切换paralog功能。

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