Understanding the importance of protein structure to nature's routes for divergent evolution in TIM barrel enzymes.
Understanding the importance of protein structure to nature's routes for divergent evolution in TIM barrel enzymes.
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了解蛋白质结构对于 TIM 桶酶趋异进化的自然途径的重要性。
DOI：
10.1021/ar030250v
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Rayment,Ivan
中科院分区：
文献类型：
--
作者：
Wise,EricL;Rayment,Ivan
人们普遍认为，新的酶是通过编码现有酶的基因的复制以及随后的序列差异而从现有酶进化而来的。虽然进化是一个固有的随机过程，但对不同相关酶的研究表明，新酶的进化遵循三种一般途径之一，其中底物特异性，反应机制或祖酶的活性位点结构在新酶中重复使用。结构生物学中与趋异相关的（β/α）8酶相关的最新进展为这些过程带来了新的见解，并揭示了保守的结构元件在趋异进化中起着重要作用。这些研究表明，虽然进化是以一系列随机突变的形式发生的，但稳定的折叠，如（β/α）8桶和酶活性位点的结构特征，在进化中经常被重复使用，并适应新的催化目的。
It is widely agreed that new enzymes evolve from existing ones through the duplication of genes encoding existing enzymes followed by sequence divergence. While evolution is an inherently random process, studies of divergently related enzymes have shown that the evolution of new enzymes follows one of three general routes in which the substrate specificity, reaction mechanism, or active site architecture of the progenitor enzyme is reused in the new enzyme. Recent developments in structural biology relating to divergently related (β/α)8 enzymes have brought new insight into these processes and have revealed that conserved structural elements play an important role in divergent evolution. These studies have shown that, although evolution occurs as a series of random mutations, stable folds such as the (β/α)8 barrel and structural features of the active sites of enzymes are frequently reused in evolution and adapted for new catalytic purposes.