The Homodimerization of Thalictrum tuberosum O-Methyltransferases by Homology-based Modelling

Bulletin of the Korean chemical society

Heejung Yang¹  Yoongho Lim¹  Karp Joo Jeong¹  Joong-Hoon Ahn¹  Sangsan Lee¹ 

关键词: Modelling;    Molecular dynamics;    Homology;    Methyltransferase;    Thalictrum tuberosum;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Two O-methyltransferases, OMTII-1 and OMTII-4 of meadow rue Thalictrum tuberosum showed a high sequence identity. Of 364 amino acids only one residue is not the same, which is Tyr21 or Cys21. Even if the 21st residues in these OMTs are not included in the binding sites of the enzymes, binding affinities of the enzyme homodimers over the same substrate are very different. While the binding affinity of one homodimer over caffeic acid is 100%, that of the other is 25%. Authors tried to predict the three-dimensional structures of Thalictrum tuberosum O-methyltransferases using homology-based modelling by a comparison with caffeic acid O-methyltransferase, and explain the reason of the phenomenon mentioned above based on their three dimensional structural studies. In the enzyme homodimer, the better binding affinity may be caused by the shorter distance between the 21st residue and the binding site of the other monomer.

【 授权许可】

Unknown