Arg305 of Streptomycesl-glutamate oxidase plays a crucial role for substrate recognition

…, C Sakaguchi, T Tamura, C Sasaki, H Kusakabe…

文献索引：Utsumi, Tomohiro; Arima, Jiro; Sakaguchi, Chika; Tamura, Takashi; Sasaki, Chiduko; Kusakabe, Hitoshi; Sugio, Shigetoshi; Inagaki, Kenji Biochemical and Biophysical Research Communications, 2012 , vol. 417, # 3 p. 951 - 955

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被引用次数: 5

摘要

Recently, we have solved the crystal structure of l-glutamate oxidase (LGOX) from Streptomyces sp. X-119-6 (PDB code: 2E1M), the substrate specificity of which is strict toward l-glutamate. By a docking simulation using l-glutamate and structure of LGOX, we selected three residues, Arg305, His312, and Trp564 as candidates of the residues associating with recognition of l-glutamate. The activity of LGOX toward l-glutamate was ...