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首页> 外文期刊>Brain research >Structural and functional evolution of 2 ',3 '-cyclic nucleotide 3 '-phosphodiesterase
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Structural and functional evolution of 2 ',3 '-cyclic nucleotide 3 '-phosphodiesterase

机译：2'，3'-环核苷酸3'-磷酸二酯酶的结构和功能进化

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摘要

2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) is an abundant membrane-associated enzyme within the vertebrate myelin sheath. While the physiological function of CNPase still remains to be characterized in detail, it is known in addition to its in vitro enzymatic activity to interact with other proteins, small molecules, and membrane surfaces. From an evolutionary point of view, it can be deduced that CNPase is not restricted to myelin forming cells or vertebrate tissues. Its evolution has involved gene fusion, addition of other small segments with distinct functions, such as membrane attachment, and possibly loss of function at the polynucleotide kinase-like domain. Currently, it is unclear whether the enzymatic function of the conserved phosphodiesterase domain in vertebrate myelin has a physiological role, or if CNPase could actually function like many other classical myelin proteins in a more structural role.
机译：2'，3'-环核苷酸3'-磷酸二酯酶（CNPase）是脊椎动物髓鞘内的一种丰富的膜相关酶。尽管CNPase的生理功能仍有待详细表征，但除了其体外酶促活性外，它还可以与其他蛋白质，小分子和膜表面相互作用。从进化的观点，可以推断出CNPase不限于髓磷脂形成细胞或脊椎动物组织。它的进化涉及基因融合，添加具有独特功能（如膜附着）的其他小片段以及可能在多核苷酸激酶样结构域丧失功能。目前，尚不清楚脊椎动物髓磷脂中保守的磷酸二酯酶结构域的酶功能是否具有生理作用，或者CNPase是否实际上可以像许多其他经典的髓磷脂蛋白一样发挥更大的结构作用。

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