L-2- ハロ酸脱ハロゲン化酵素の立体構造と反応機構の解析 Crystallographic Analysis of the Tertiary Structure and Reaction Mechanism of L-2-Haloacid Dehalogenase
The structure and function of homodimeric L-2-haloacid dehalogenase from <I>Pseudomonas</I> sp. YL has been investigated by X-ray crystallographic methods. Each subunit of the enzyme consists of two domains. The core domain has a unique α/β structure which is different from the α/βhydrolase fold, and contains almost all the active site residues. The subdomain for dimerization has a four-helix bundle structure. The structure analysis of the complex between the S175A mutant and L-2-chlorobutyrate has revealed the structure of the corresponding ester intermediate. This suggests that the catalysis of the enzyme must proceed in SN2 substitution reaction via the ester intermediate.
日本結晶学会誌 39(5), 358-365, 1997-10
The Crystallographic Society of Japan