초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 09월 03일 23시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제122회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Crystal structure and functional characterization of a novel FAH (fumarylacetoacetate hydrolase) family hydrolase from Exiguobacterium antarcticum DSM

2018년 8월 30일 13시 29분 21초
LIFE.P-453 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 19일 (금요일) 11:00~12:30
Life Chemistry
저자 및
Wanki Yoo, Doo Hun Kim1,*
College of Medicine, Sungkyunkwan University, Korea
1Department of Chemistry, Sookmyung Women's University, Korea
A novel hydrolase, EaD30 from psychrophilic bacteria, Exiguobacterium antarcticum DSM were identified and characterized. Multiple sequence alignment with the sequences retrieved from PSI-BLAST revealed that EaD30 belongs to FAH (fumarylacetoacetate hydrolase) family. Genetic analysis of EaD30 locus confirmed that neighboring genes including EaD30 gene were highly conserved across Exiguobacterium strains indicating that EaD30 has an important role for the strains. Previously, few FAHs were identified and crystallized. Sequence alignment and the crystal structure of the FAHs showed that putative catalytic site, His and Glu, were well conserved and located in a HxxE motif in the lid domain. However, the catalytic lid domain is missing in most crystal structures of the native FAHs, making it hard to elucidate molecular mechanism of catalysis by FAHs. Here, we report the crystal structure of EaD30. In the crystal structure of EaD30, the catalytic lid domain was well defined without any stabilization by substrates. Furthermore, biochemical and biophysical characters of EaD30 were studied using spectrofluorometry, circular dichroism (CD), non-denaturing PAGE, and gel filtration chromatography. Collectively, the structure of EaD30 and biochemical results will pave a way to explain the role of the catalytic lid domain in the catalysis of FAHs