| Title : The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates - Shinohara_2014_FEBS.Lett_588_995 |
| Author(s) : Shinohara Y , Miyanaga A , Kudo F , Eguchi T |
| Ref : FEBS Letters , 588 :995 , 2014 |
|
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 alpha/beta hydrolase type serine peptidases. |
| PubMedSearch : Shinohara_2014_FEBS.Lett_588_995 |
| PubMedID: 24530530 |
| Gene_locus related to this paper: strha-q76ky6 |
| Substrate | N-alanyl-secovicenilactam-ethyl-ester |
| Gene_locus | strha-q76ky6 |
| Structure | 3WMR |
Shinohara Y, Miyanaga A, Kudo F, Eguchi T (2014)
The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates
FEBS Letters
588 :995
Shinohara Y, Miyanaga A, Kudo F, Eguchi T (2014)
FEBS Letters
588 :995