aspartate racemase
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PLoS ONE ◽  
2020 ◽  
Vol 15 (1) ◽  
pp. e0228178 ◽  
Author(s):  
Tania Henríquez ◽  
Juan Carlos Salazar ◽  
Massimiliano Marvasi ◽  
Ajit Shah ◽  
Gino Corsini ◽  
...  

2020 ◽  
Vol 169 ◽  
pp. 112164 ◽  
Author(s):  
Kouji Uda ◽  
Yumika Edashige ◽  
Rie Nishimura ◽  
Yuuna Shikano ◽  
Tohru Matsui ◽  
...  
Keyword(s):  

2019 ◽  
Vol 84 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Kimihiko Shibata ◽  
Noriko Sugaya ◽  
Yuko Kuboki ◽  
Hiroko Matsuda ◽  
Katsumasa Abe ◽  
...  
Keyword(s):  

2019 ◽  
Vol 514 (4) ◽  
pp. 1108-1114 ◽  
Author(s):  
Dong-Dong Cao ◽  
Chun-Peng Zhang ◽  
Kang Zhou ◽  
Yong-Liang Jiang ◽  
Xiao-Feng Tan ◽  
...  

2018 ◽  
Vol 200 (15) ◽  
Author(s):  
Mark J. Mandel

ABSTRACT Work by Jones et al. (R. M. Jones, Jr., D. L. Popham, A. L. Schmidt, E. L. Neidle, and E. V. Stabb, J Bacteriol 200:e00773-17, 2018, https://doi.org/10.1128/JB.00773-17) describes a d-aspartate-sensing system in proteobacteria. d-Amino acids are critical components of peptidoglycan and other structures. The new study identifies the LysR-type transcriptional regulator DarR, which activates the aspartate racemase RacD. The overexpression of RacD enables it to synthesize d-glutamate and restore normal peptidoglycan in a Vibrio fischeri murI mutant. This study contributes to the understanding of emerging roles for d-amino acids and how they are synthesized under distinct conditions.


Author(s):  
Taichi Mizobuchi ◽  
Risako Nonaka ◽  
Motoki Yoshimura ◽  
Katsumasa Abe ◽  
Shouji Takahashi ◽  
...  

Aspartate racemase (AspR) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that is responsible for D-aspartate biosynthesis in vivo. To the best of our knowledge, this is the first study to report an X-ray crystal structure of a PLP-dependent AspR, which was resolved at 1.90 Å resolution. The AspR derived from the bivalve mollusc Scapharca broughtonii (SbAspR) is a type II PLP-dependent enzyme that is similar to serine racemase (SR) in that SbAspR catalyzes both racemization and dehydration. Structural comparison of SbAspR and SR shows a similar arrangement of the active-site residues and nucleotide-binding site, but a different orientation of the metal-binding site. Superposition of the structures of SbAspR and of rat SR bound to the inhibitor malonate reveals that Arg140 recognizes the β-carboxyl group of the substrate aspartate in SbAspR. It is hypothesized that the aromatic proline interaction between the domains, which favours the closed form of SbAspR, influences the arrangement of Arg140 at the active site.


Amino Acids ◽  
2017 ◽  
Vol 49 (10) ◽  
pp. 1743-1754 ◽  
Author(s):  
Kouji Uda ◽  
Keita Abe ◽  
Yoko Dehara ◽  
Kiriko Mizobata ◽  
Yumika Edashige ◽  
...  

Extremophiles ◽  
2016 ◽  
Vol 20 (4) ◽  
pp. 385-393 ◽  
Author(s):  
Takayuki Aihara ◽  
Toshiya Ito ◽  
Yasuaki Yamanaka ◽  
Keiichi Noguchi ◽  
Masafumi Odaka ◽  
...  

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