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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Development of 'substrate-trapping' mutants to identify physiological substrates of protein tyrosine phosphatases
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Development of 'substrate-trapping' mutants to identify physiological substrates of protein tyrosine phosphatases

机译:“底物捕获”突变体的开发,以鉴定蛋白质酪氨酸磷酸酶的生理底物

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摘要

The identification of substrates of protein ty- rosine phosphatases (PTPs) is an essential step toward a com- plete understanding of the physiological function of members of this enzyme family. PTPs are defined by a conserved catalytic domain harboring 27 invariant residues. From a mutagenesis study of these invariant residues that was guided by our knowl- edge of the crystal structure of PTP1B, we have discovered a mutation of the invariant catalytic acid (Asp-181 in PTP1B) that converts an extremely active enzyme into a "substrate trap."
机译:蛋白质酪氨酸磷酸酶(PTP)底物的鉴定是全面了解该酶家族成员生理功能的重要步骤。 PTP由保守的催化结构域定义,该结构域包含27个不变残基。根据我们对PTP1B晶体结构知识的了解,对这些恒定残基进行了诱变研究,我们发现了恒定催化酸(PTP1B中的Asp-181)发生了突变,该突变将一种极为活跃的酶转化为“底物”。陷阱。”

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