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Publication Abstract from PubMed

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 beta-sandwich roll fold with a highly flexible lid region (Val(73)-Leu(94)), and an Mg(2+) ion is bound at the active site by coordinating to the three carboxylate oxygen atoms of Glu(124), Glu(126), and Asp(155). 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.

Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.,Yoo W, Lee CW, Kim BY, Huong Luu Le LT, Park SH, Kim HW, Shin SC, Kim KK, Lee JH, Kim TD Biochem Biophys Res Commun. 2019 Feb 12;509(3):773-778. doi:, 10.1016/j.bbrc.2018.12.183. Epub 2019 Jan 8. PMID:30630595^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.