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

Biochem. Biophys. Res. Commun.2018 Sep 18;503(4):2319-2325. Epub 2018 Jun 30
Hui Dong 1 , Qingqing Han 2 , Yu Guo 3 , Jiansong Ju 2 , Shanshan Wang 4 , Chao Yuan 3 , Wei Long 1 , Xin He 1 , Shujing Xu 5 , Sheng Li 6
Hui Dong 1 , Qingqing Han 2 , Yu Guo 3 , Jiansong Ju 2 , Shanshan Wang 4 , Chao Yuan 3 , Wei Long 1 , Xin He 1 , Shujing Xu 5 , Sheng Li 6
+ et al

[No authors listed]

Author information
  • 1 Key Laboratory of Tianjin Radiation and Molecular Nuclear Medicine, Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin, 300192, China.
  • 2 College of Life Science, Hebei Normal University, Shijiazhuang, 050024, China.
  • 3 Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China; University of Chinese Academy of Sciences, Beijing, 100049, China; School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
  • 4 Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China.
  • 5 College of Life Science, Hebei Normal University, Shijiazhuang, 050024, China. Electronic address: josyokei@163.com.
  • 6 Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China. Electronic address: lisheng@shanghaitech.edu.cn.

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.

KEYWORDS: Alanine racemase, Biosynthetic, Homodimer, Pseudomonas aeruginosa PAO1

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