Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum
- Authors
- Yoo, Wanki; Lee, Chang Woo; Kim, Boo-young; Ly Thi Huong Luu Le; Park, Sun-Ha; Kim, Han-Woo; Shin, Seung Chul; Kim, Kyeong Kyu; Lee, Jun Hyuck; Kim, T. Doohun
- Issue Date
- Feb-2019
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- EaFAH; Fumarylacetoacetate hydrolase; Exiguobacterium antarcticum
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.509, no.3, pp 773 - 778
- Pages
- 6
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 509
- Number
- 3
- Start Page
- 773
- End Page
- 778
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/3839
- DOI
- 10.1016/j.bbrc.2018.12.183
- ISSN
- 0006-291X
1090-2104
- 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 beta-sandwich roll fold with a highly flexible lid region (Val(73)-Leu(94)), and an Mg2+ 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. (C) 2019 Elsevier Inc. All rights reserved.
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