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首页> 外文期刊>The FEBS journal >The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles - Ser195 and Cys145 are predicted to be the active site nucleophiles
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The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles - Ser195 and Cys145 are predicted to be the active site nucleophiles

机译：来自Sulfolobus solfataricus的标志性酰胺酶属于能裂解酰胺和腈的酶的CX3C亚组-预计Ser195和Cys145是活性位点亲核试剂

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摘要

The signature amidase from the extremophile archeum Sulfolobus solfataricus is an enantioselective enzyme that cleaves S-amides. We report here that this enzyme also converts nitriles in the corresponding organic acid, similarly to the well characterized amidase from Rhodococcus rhodochrous J1. The archaeal and rhodococcal enzymes belong to the signature amidases and contain the typical serine-glycine rich motif. They work at different optimal temperature, share a high sequence similarity and both contain an additional CX3C motif. To explain their dual specificity, we built a 3D model of the structure of the S. solfataricus enzyme, which suggests that, in addition to the classical catalytic Ser-cisSer-Lys, a putative additional Cys-cisSer-Lys catalytic site, likely to be responsible for nitrile hydrolysis, is present in these proteins. The results of random and site-directed mutagenesis experiments, as well as inhibition studies support our hypothesis.
机译：来自极端嗜热菌古菌Sulfolobus solfataricus的特征性酰胺酶是一种裂解S-酰胺的对映选择性酶。我们在这里报告说，该酶还可以将相应的有机酸转化为腈，类似于来自红球红球菌J1的酰胺酶。古细菌和红球菌属酶属于标志性酰胺酶，并含有典型的富含丝氨酸-甘氨酸的基序。它们在不同的最佳温度下工作，具有高度的序列相似性，并且都包含一个额外的CX3C基序。为了解释它们的双重特异性，我们建立了S. solfataricus酶结构的3D模型，这表明，除了经典的催化Ser-cisSer-Lys之外，推定的其他Cys-cisSer-Lys催化位点可能这些蛋白质中存在负责腈水解的物质。随机和定点诱变实验的结果以及抑制研究均支持我们的假设。

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