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首页> 外文期刊>FEBS Open Bio >Carboxypeptidase Y activity and maintenance is modulated by a large helical structure
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Carboxypeptidase Y activity and maintenance is modulated by a large helical structure

机译：羧肽酶Y的活性和维持受大的螺旋结构调节

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摘要

Yeast carboxypeptidase Y (CPY) is a serine protease with broad substrate specificity. Structurally, CPY belongs to the α/β hydrolase fold family and contains characteristic large helices, termed the V‐shape helix, above the active site cavity. Four intramolecular disulfide bonds are located in and around the V‐shape helix. In this study, mutant CPYs were constructed in which one of these disulfide bonds was disrupted. Mutants lacking the C193–C207 bond located at the beginning of the V‐shape helix aggregated easily, while mutants lacking the C262–C268 bond located at the end of the V‐shape helix displayed decreased hydrolytic activity. The results indicate that the V‐shape helix is involved in CPY catalysis and in maintenance of its conformation.
机译：酵母羧肽酶Y（CPY）是一种具有广泛底物特异性的丝氨酸蛋白酶。从结构上讲，CPY属于α/β水解酶折叠家族，在活动位点腔上方包含特征性大螺旋，称为V型螺旋。四个分子内二硫键位于V形螺旋内和周围。在这项研究中，构建了突变CPY，其中这些二硫键之一被破坏。缺少位于V形螺旋末端的C193–C207键的突变体容易聚集，而缺少位于V形螺旋末端的C262–C268键的突变体表现出降低的水解活性。结果表明，V形螺旋参与CPY催化并维持其构象。

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