The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates.

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 Lett

journal_title

FEBS letters

authors

Shinohara Y,Miyanaga A,Kudo F,Eguchi T

doi

10.1016/j.febslet.2014.01.060

subject

Has Abstract

pub_date

2014-03-18 00:00:00

pages

995-1000

issue

6

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00103-3

journal_volume

588

pub_type

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