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Crystal structures clarify cofactor binding of plant tyrosine decarboxylase
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| Title: | Crystal structures clarify cofactor binding of plant tyrosine decarboxylase |
| Authors: | Wang, Hang Browse this author | | Yu, Jian Browse this author | | Satoh, Yasuharu Browse this author | | Nakagawa, Yusuke Browse this author | | Tanaka, Ryusuke Browse this author | | Kato, Koji Browse this author | | Yao, Min Browse this author →KAKEN DB |
| Keywords: | Plant tyrosine decarboxylase | | Aromatic amino acid decarboxylases | | PLP-dependent | | Structure |
| Issue Date: | 5-Mar-2020 |
| Publisher: | Elsevier |
| Journal Title: | Biochemical and biophysical research communications |
| Volume: | 523 |
| Issue: | 2 |
| Start Page: | 500 |
| End Page: | 505 |
| Publisher DOI: | 10.1016/j.bbrc.2019.12.077 |
| Abstract: | Plant tyrosine decarboxylase (TyrDC) is a group II pyridoxal 5'-phosphate (PLP)-dependent decarboxylase that mainly catalyzes the decarboxylation of tyrosine to tyramine. This is biologically important for diverting essential primary metabolites into secondary metabolic pathways. Intensive studies have characterized the effective of PLP-binding and the substrate specificity of mammalian 3,4-dihydroxyphenyl-L-alanine (Dopa) decarboxylases, a member of group II PLP-dependent decarboxylase. However, the characteristics of PLP binding and substrate specificity of plant TyrDCs remain unknown. In this study, we focus on the PLP binding manner, and determined the crystal structures of the apo and PLP binding form of type II TyrDC from Papaver somniferum (PsTyrDCII and PsTyrDCII-PLP). The structures showed that, unlike mammalian Dopa decarboxylase, the binding of PLP does not induce distinct conformational changes of PsTyrDCII regarding the overall structure, but the PLP binding pocket displays conformational changes at Phe124, His203 and Thr262. Combining structural comparation and the obtained biochemical findings, it is demonstrated that PsTyrDCII does not binds PLP tightly. Such characteristics of PLP binding may be required by its catalytic reaction and substrate binding. The activity of TyrDC probably regulated by the concentration of PLP in cells. (C) 2019 The Authors. Published by Elsevier Inc. |
| Rights: | http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/78369 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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