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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural characteristics of thermoactive L-Arabinose Isomerase from Geobacillus Kaustophilus

2014년 9월 4일 16시 58분 03초
PHYS.P-492 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 15일 (수요일) 16:00~19:00
저자 및
김철희, 김은애*
조선대학교 약학과, Korea
GKAI (Geobacillus Kaustophilus Arabinose Isomerase; L-AI) is an enzyme to convert L-arabinose into L-ribulose in vivo and has high activity and stability at 60 ℃. Though L-AI structure was solved by X-ray, the experimental temperature as 20℃ is not reliable to understand a mechanism of the thermoactive enzyme. Therefore, molecular dynamics simulation is performed at the active temperature using GROMCAS software. The monomer consists of 493 amino acid residues and a total system is a trimer with TIP3p water box. The protein system is modelled by amber99sb-nmr-ildn force field. Since the ligand sbbinding site with a metal (Mn2+) is located at monomer boundary surface, monomer-monomer interaction would be important to open the enzyme gate. According to the simulation results, it is shown that the hydrophobic core between helixs as the tertiary structure is broken in the boundary of a monomer and the monomer secondary structure is still conserved. In the opposite side of the other monomer with a metal binding site , a hydrophobic core formed by loops is rearranged as a new hydrophobic core. To conform the opening mechanism of L-AI, we run the single mutation simulation with modification of Tyr20 into Ala20. However, there was no remarkable difference between the two results and then we try to run other simulations with other residues.