title: 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.
abstract: 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 epsilon2 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 gamma.
authors.affiliation: Department of Biotechnology, School of Engineering, Nagoya University, Chikusa, Nagoya 464-8603, Japan.
authors.forename: Seiji
authors.initials: S
authors.lastname: Okazaki
authors.forename: Atsuo
authors.initials: A
authors.lastname: Suzuki
authors.forename: Tsunehiro
authors.initials: T
authors.lastname: Mizushima
authors.forename: Hidenobu
authors.initials: H
authors.lastname: Komeda
authors.forename: Yasuhisa
authors.initials: Y
authors.lastname: Asano
authors.forename: Takashi
authors.initials: T
authors.lastname: Yamane
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D020621:Ochrobactrum anthropi / Q000201:enzymology*; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D010649:Phenylalanine; C020457:phenylalanine amide; D000581:Amidohydrolases; C019665:amidase