Coumarins belong to an important class of plant secondary metabolites. Feruloyl-CoA 6’-hydroxylase (F6’H), a 2-oxoglutarate dependent dioxygenase (2OGD), catalyzes a pivotal step in the biosynthesis of a simple coumarin scopoletin. In this study, we determined the 3-dimensional structure of the F6’H1 apo enzyme by X-ray crystallography. It is the first reported structure of a 2OGD enzyme involved in coumarin biosynthesis and closely resembles the structure of Arabidopsis thaliana anthocyanidin synthase. To better understand the mechanism of enzyme catalysis and substrate specificity, we also generated a homology model of a related ortho-hydroxylase (C2’H) from sweet potato. By comparing these two structures, we targeted two amino acid residues and verified their roles in substrate binding and specificity by site-directed mutagenesis.
Structural Insights into Substrate Specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana
Xinxiao Sun,Dayong Zhou,P. Kandavelu,Hua Zhang,Qipeng Yuan,Bi-Cheng Wang,J. Rose,Yajun Yan
Published 2015 in Scientific Reports
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- Publication year
2015
- Venue
Scientific Reports
- Publication date
2015-05-20
- Fields of study
Biology, Medicine, Chemistry, Environmental Science
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Semantic Scholar, PubMed
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