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首页> 外文期刊>Journal of bacteriology >Specific in vivo cleavage of D-serine deaminase and properties of tetrameric polypeptide aggregates of the fragments.
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Specific in vivo cleavage of D-serine deaminase and properties of tetrameric polypeptide aggregates of the fragments.

机译:D-丝氨酸脱氨酶的特异性体内切割和片段的四聚体多肽聚集体的性质。

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摘要

The primary D-serine deaminase (D-serine dehydratase, EC 4.2.1.14) of Escherichia coli K-12 is unstable within the cell. The protein, a single polypeptide chain, is cleaved at a lysine residue by a cellular proteolytic activity. Fragments containing the active site then aggregate into tetramers, which retain substrate affinity and show very low catalytic activity. Such degradations may represent an evolutionary mechanism for the generation of new enzymes.
机译:大肠杆菌K-12的主要D-丝氨酸脱氨酶(D-丝氨酸脱水酶,EC 4.2.1.14)在细胞内不稳定。该蛋白质为一条多肽链,通过细胞蛋白水解活性在赖氨酸残基处裂解。然后,含有活性位点的片段聚集成四聚体,四聚体保留了底物亲和力并显示出非常低的催化活性。此类降解可能代表了新酶生成的进化机制。

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