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
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
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DOI：
10.1107/s0907444907067479
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发表时间：
2008-03-01
期刊：
影响因子：
--
通讯作者：
Yamane, Takashi
中科院分区：
文献类型：
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作者：
Okazaki, Seiji;Suzuki, Atsuo;Yamane, Takashi
分别以 2.3 和 2.2 埃的分辨率测定了来自人苍白杆菌 SV3 的 D-氨基酸酰胺酶 (DAA) 与 L-苯丙氨酸和 L-苯丙氨酸酰胺复合物的晶体结构。 L-苯丙氨酸酰胺复合物与D-苯丙氨酸复合物的比较表明，DAA的D-立体专一性可能是由于三个结构因素而实现的：（i）底物疏水侧链所在区域的疏水空腔，（ii）固定底物氨基N原子的Gln310 O和Glu114 O-epsilon 2的空间排列，以及（iii）保持底物疏水侧链的两个空腔的存在。底物的羧基/酰胺基团靠近或远离 Ser60 O-γ。
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 angstrom 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-epsilon 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-gamma.