2 reference(s) found. Listing paper details in reverse chronological order. We are grateful to Keith Bradnam for improvment of this script
Title: The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates Shinohara Y, Miyanaga A, Kudo F, Eguchi T Ref: FEBS Letters, 588:995, 2014 : PubMed
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.
        
Title: A natural protecting group strategy to carry an amino acid starter unit in the biosynthesis of macrolactam polyketide antibiotics Shinohara Y, Kudo F, Eguchi T Ref: Journal of the American Chemical Society, 133:18134, 2011 : PubMed
Macrolactam antibiotics are an important class of macrocyclic polyketides that contain a unique nitrogen-containing starter unit. In the present study, a set of starter biosynthetic enzymes in the macrolactam antibiotic vicenistatin was characterized. We found that the protection-deprotection strategy of the aminoacyl-ACP intermediate was critical in this system. On the basis of bioinformatics, the described pathway is also proposed as a common method for carrying amino acids in the biosynthesis of other macrolactam antibiotics.