Enhancement of the thermostability and catalytic activity of d-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 by directed evolution

Structures of d-amino-acid amidase compl

Structures of d-amino-acid amidase complexed with l-phenylalanine and with l-phenylalanine amide: insight into the d-stereospecificity of d-amino-acid amidase from Ochrobactrum anthropi SV3

✍ Okazaki, Seiji ;Suzuki, Atsuo ;Mizushima, Tsunehiro ;Komeda, Hidenobu ;Asano, Ya 📂 Article 📅 2008 🏛 International Union of Crystallography 🌐 English ⚖ 608 KB

The crystal structures of d-amino-acid amidase (DAA) from Ochrobactrum anthropi SV3 in complex with l-phenylalanine and with l-phenylalanine amide were determined at 2.3 and 2.2 A ˚resolution, respectively. Comparison of the l-phenylalanine amide complex with the d-phenylalanine complex reveals that