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
1997 年 39 巻 5 号 p. 358-365
詳細
1997 年 39 巻 5 号 p. 358-365
The structure and function of homodimeric L-2-haloacid dehalogenase from Pseudomonas 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.
