7XWT

Crystal structure of Feruoyl-CoA hydratase/lyase complexed with CoA from Sphingomonas paucimobilis

7XWT の概要

• エントリーDOI: 10.2210/pdb7xwt/pdb
• 分子名称: Feruloyl-CoA hydratase/lyase, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: feruloyl-coa hydratase/lyase, lyase
• 由来する生物種: Sphingomonas paucimobilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34422.67

構造登録者

Seok, J.,Kim, K.-J. (登録日: 2022-05-27, 公開日: 2023-01-18, 最終更新日: 2023-11-29)

主引用文献

Seok, J.,Seo, H.,Hong, J.,Kim, K.J.
Production of various phenolic aldehyde compounds using the 4CL-FCHL biosynthesis platform.
Int.J.Biol.Macromol., 226:608-617, 2023

PubMed Abstract: Vanillin (3-methoxy-4-hydroxybenzaldehyde) is one of the most important flavoring substances used in the cosmetic and food industries. Feruloyl-CoA hydratase/lyase (FCHL) is an enzyme that catalyzes the production of vanillin from feruloyl-CoA. In this study, we report kinetic parameters and biochemical properties of FCHL from Sphingomonas paucimobilis SYK-6 (SpFCHL). Also, the crystal structures of an apo-form of SpFCHL and two complexed forms with acetyl-CoA and vanillin/CoA was present. Comparing the apo structure to its complexed forms of SpFCHL, a gate loop with an "open and closed" role was observed at the entrance of the substrate-binding site. With vanillin and CoA complexed to SpFCHL, we captured a conformational change in the feruloyl moiety-binding pocket that repositions the catalytic SpFCHL and other key residues. This binding pocket does not tightly fit the vanillin structure, suggesting substrate promiscuity of this enzyme. This observation is in good agreement with assay results for phenylpropanoid-CoAs and indicates important physicochemical properties of the substrate for the hydratase/lyase reaction mechanism. In addition, we showed that various phenolic aldehydes could be produced using the 4CL-FCHL biosynthesis platform.

PubMed: 36521700
DOI: 10.1016/j.ijbiomac.2022.12.075

実験手法

X-RAY DIFFRACTION (1.76 Å)