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Title: Structural insights into substrate specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana

Abstract

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 (C 2’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.

Authors:
 [1];  [2];  [2];  [2];  [1];  [2];  [2];  [2]
  1. Beijing Univ. of Chemical Technology, Beijing (China)
  2. Univ. of Georgia, Athens, GA (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1215409
Grant/Contract Number:  
W-31-109-ENG-38
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Scientific Reports
Additional Journal Information:
Journal Volume: 5; Journal ID: ISSN 2045-2322
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; biocatalysis; enzyme mechanisms; enzymes; X-ray crystallography

Citation Formats

Sun, Xinxiao, Zhou, Dayong, Kandavelu, Palani, Zhang, Hua, Yuan, Qipeng, Wang, Bi -Cheng, Rose, John, and Yan, Yajun. Structural insights into substrate specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana. United States: N. p., 2015. Web. doi:10.1038/srep10355.
Sun, Xinxiao, Zhou, Dayong, Kandavelu, Palani, Zhang, Hua, Yuan, Qipeng, Wang, Bi -Cheng, Rose, John, & Yan, Yajun. Structural insights into substrate specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana. United States. doi:10.1038/srep10355.
Sun, Xinxiao, Zhou, Dayong, Kandavelu, Palani, Zhang, Hua, Yuan, Qipeng, Wang, Bi -Cheng, Rose, John, and Yan, Yajun. Wed . "Structural insights into substrate specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana". United States. doi:10.1038/srep10355. https://www.osti.gov/servlets/purl/1215409.
@article{osti_1215409,
title = {Structural insights into substrate specificity of Feruloyl-CoA 6’-Hydroxylase from Arabidopsis thaliana},
author = {Sun, Xinxiao and Zhou, Dayong and Kandavelu, Palani and Zhang, Hua and Yuan, Qipeng and Wang, Bi -Cheng and Rose, John and Yan, Yajun},
abstractNote = {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.},
doi = {10.1038/srep10355},
journal = {Scientific Reports},
issn = {2045-2322},
number = ,
volume = 5,
place = {United States},
year = {2015},
month = {5}
}

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