The Crystal Structure of the Amidohydrolase VinJ Shows a Unique Hydrophobic Tunnel for its Interaction with Polyketide Substrates
The Crystal Structure of the Amidohydrolase VinJ Shows a Unique Hydrophobic Tunnel for its Interaction with Polyketide Substrates
复制标题
酰胺水解酶 VinJ 的晶体结构显示出与聚酮化合物底物相互作用的独特疏水通道
DOI：
10.1016/j.febslet.2014.01.060
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Tadashi Eguchi
中科院分区：
文献类型：
--
作者：
Yuji Shinohara;Akimasa Miyanaga;Fumitaka Kudo;Tadashi Eguchi
VinJ是一种属于丝氨酸肽酶家族的酰胺水解酶，其在维西他汀的生物合成期间催化聚酮化合物中间体的末端氨酰基部分的水解。在此，我们报告的晶体结构的VinJ。VinJ具有独特的疏水通道，用于识别其底物在帽结构域中的聚酮化合物链部分。结合系统发育分析的结果，我们的结果表明VinJ代表了一个新的酰胺水解酶家族，不同于已知的α/β水解酶型丝氨酸肽酶。
VinJ is an amidohydrolase belonging to the serine peptidase family that catalyzes the hydrolysis of the terminal aminoacyl moiety of a polyketide intermediate during the biosynthesis of vicenistatin. Herein, we report the crystal structure of VinJ. VinJ possesses a unique hydrophobic tunnel for the recognition of the polyketide chain moiety of its substrate in the cap domain. Taken together with the results of phylogenetic analysis, our results suggest that VinJ represents a new amidohydrolase family that is different from the known α/β hydrolase type serine peptidases.