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The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates |
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| Authors: | Yuji Shinohara Akimasa Miyanaga Fumitaka Kudo Tadashi Eguchi |
| Institution: | 1. Department of Chemistry and Materials Science, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan;2. Department of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan |
| Abstract: | 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. |
| Keywords: | ACP acyl carrier protein pNA p-nitroanilide r m s d root mean square deviation F1 tricon-interacting peptidase F1 PIP proline iminopeptidase PAP prolyl aminopeptidase |
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