Enzymatic characterization and crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1

被引：3
|
作者：
Dong, Hui [1 ,2 ]
Han, Qingqing [3 ]
Guo, Yu [4 ,5 ,6 ]
Ju, Jiansong [3 ]
Wang, Shanshan [4 ]
Yuan, Chao [4 ,5 ,6 ]
Long, Wei [1 ,2 ]
He, Xin [1 ,2 ]
Xu, Shujing [3 ]
Li, Sheng [4 ]
机构：
[1] Chinese Acad Med Sci, Inst Radiat Med, Key Lab Tianjin Radiat & Mol Nucl Med, Tianjin 300192, Peoples R China
[2] Peking Union Med Coll, Tianjin 300192, Peoples R China
[3] Hebei Normal Univ, Coll Life Sci, Shijiazhuang 050024, Hebei, Peoples R China
[4] ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China
[5] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[6] ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2018年 / 503卷 / 04期
关键词：
Alanine racemase; Pseudomonas aeruginosa PAO1; Biosynthetic; Homodimer; D-AMINO ACIDS; BACILLUS-STEAROTHERMOPHILUS; ESCHERICHIA-COLI; X-RAY; GROWTH; TUBERCULOSIS; MECHANISM; MUTANTS; BINDS; GENE;
D O I：
10.1016/j.bbrc.2018.06.155
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Alanine racemase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that reversibly catalyzes the conversion of L-alanine to D-alanine. D-alanine is an essential constituent in many prokaryotic cell structures. Inhibition of alanine racemase is lethal to prokaryotes, creating an attractive target for designing antibacterial drugs. Here we report the crystal structure of biosynthetic alanine racemase (Alr) from a pathogenic bacteria Pseudomonas aeruginosa PAO1. Structural studies showed that P. aeruginosa Alr (PaAlr) adopts a conserved homodimer structure. A guest substrate D-lysine was observed in the active site and refined to dual-conformation. Two buffer ions, malonate and acetate, were bound in the proximity to D-lysine. Biochemical characterization revealed the optimal reaction conditions for PaAlr. (C) 2018 Elsevier Inc. All rights reserved.
引用
收藏
页码：2319 / 2325
页数：7
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