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
✍ Scribed by Okazaki, Seiji ;Suzuki, Atsuo ;Mizushima, Tsunehiro ;Komeda, Hidenobu ;Asano, Yasuhisa ;Yamane, Takashi
- Publisher
- International Union of Crystallography
- Year
- 2008
- Tongue
- English
- Weight
- 608 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0907-4449
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✦ Synopsis
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 the d-stereospecificity of DAA might be achieved as a consequence of three structural factors: (i) the hydrophobic cavity in the region in which the hydrophobic side chain of the substrate is held, (ii) the spatial arrangement of Gln310 O and Glu114 O "2 that fixes the amino N atom of the substrate and (iii) the existence of two cavities that keep the carboxyl/amide group of the substrate near or apart from Ser60 O .