- 作者: Hsuan-Liang Liu Yih Ho Chia-Ming Hsu
- 作者服務機構: Department of Chemical Engineering, National Taipei University of Technology and School of Pharmacy, Taipei Medical University, Taipei, Taiwan, ROC
- 中文摘要: --
- 英文摘要:
Molecular docking simulations were performed in this
study to investigate the importance of both structural
and catalytic zinc ions in the human alcohol dehydroge-
nase β β on substrate binding. The structural zinc ion is
not only important in maintaining the structural integrity
of the enzyme, but also plays an important role in deter-
mining substrate binding. The replacement of the cata-
lytic zinc ion or both catalytic and structural zinc ions with
Cu results in better substrate binding affinity than with
the wild-type enzyme. The width of the bottleneck
formed by L116 and V294 in the substrate binding pocket
plays an important role for substrate entrance. In addi-
tion, unfavorable contacts between the substrate and
T48 and F93 prevent the substrate from moving too close
to the metal ion. The optimal binding position occurs
between 1.9 and 2.4 A from the catalytic metal ion.
a - 中文關鍵字: --
- 英文關鍵字: Alochol dehydrogenase. Binding affinity. Docking. Substrate binding pocket. Zinc ion