6IYM

Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum

6IYM の概要

• エントリーDOI: 10.2210/pdb6iym/pdb
• 分子名称: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: fumarylacetoacetate hydrolase, exiguobacterium antarctica, hydrolase
• 由来する生物種: Exiguobacterium antarcticum B7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63240.02

構造登録者

Lee, J.H.,Lee, C.W. (登録日: 2018-12-17, 公開日: 2019-04-03, 最終更新日: 2024-03-27)

主引用文献

Yoo, W.,Lee, C.W.,Kim, B.Y.,Huong Luu Le, L.T.,Park, S.H.,Kim, H.W.,Shin, S.C.,Kim, K.K.,Lee, J.H.,Kim, T.D.
Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.
Biochem. Biophys. Res. Commun., 509:773-778, 2019

PubMed Abstract: Fumarylacetoacetate hydrolase (FAH) is essential for the degradation of aromatic amino acids as well as for the cleavage of carbon-carbon bonds in metabolites or small organic compounds. Here, the X-ray crystal structure of EaFAH, a dimeric fumarylacetoacetate hydrolase from Exiguobacterium antarcticum, was determined, and its functional properties were investigated using biochemical methods. EaFAH adopts a mixed β-sandwich roll fold with a highly flexible lid region (Val-Leu), and an Mg ion is bound at the active site by coordinating to the three carboxylate oxygen atoms of Glu, Glu, and Asp. The hydrolytic activity of EaFAH toward various substrates, including linalyl acetate was investigated using native polyacrylamide gel electrophoresis, activity staining, gel filtration, circular dichroism spectroscopy, fluorescence, and enzyme assays.

PubMed: 30630595
DOI: 10.1016/j.bbrc.2018.12.183

実験手法

X-RAY DIFFRACTION (2.1 Å)