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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Shinohara Y,Miyanaga A,Kudo F,Eguchi Tdoi
10.1016/j.febslet.2014.01.060subject
Has Abstractpub_date
2014-03-18 00:00:00pages
995-1000issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00103-3journal_volume
588pub_type
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