scholarly journals d-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia

2007 ◽  
Vol 26 (6) ◽  
pp. 1657-1669 ◽  
Author(s):  
Louise Verrall ◽  
Mary Walker ◽  
Nancy Rawlings ◽  
Isabel Benzel ◽  
James N. C. Kew ◽  
...  
2021 ◽  
Vol 1751 ◽  
pp. 147202
Author(s):  
Shunsuke Takagi ◽  
Darrick T. Balu ◽  
Joseph T. Coyle

2006 ◽  
Vol 540 (1-3) ◽  
pp. 82-86 ◽  
Author(s):  
Kazuhide Takeyama ◽  
Masanobu Yoshikawa ◽  
Tetsuo Oka ◽  
Mitsuru Kawaguchi ◽  
Toshiyasu Suzuki ◽  
...  

2014 ◽  
Vol 5 (9) ◽  
pp. 848-854 ◽  
Author(s):  
Gabriel E. Romero ◽  
Amber D. Lockridge ◽  
Catherine W. Morgans ◽  
Dipankar Bandyopadhyay ◽  
Robert F. Miller

2007 ◽  
Vol 555 (1) ◽  
pp. 17-22 ◽  
Author(s):  
Atsushi Hashimoto ◽  
Masanobu Yoshikawa ◽  
Hidehiro Andoh ◽  
Hiroshi Yano ◽  
Hideo Matsumoto ◽  
...  

Amino Acids ◽  
2012 ◽  
Vol 43 (5) ◽  
pp. 1919-1931 ◽  
Author(s):  
Yurika Miyoshi ◽  
Ryuichi Konno ◽  
Jumpei Sasabe ◽  
Kyoko Ueno ◽  
Yosuke Tojo ◽  
...  

2005 ◽  
Vol 525 (1-3) ◽  
pp. 94-97 ◽  
Author(s):  
Masanobu Yoshikawa ◽  
Hidehiro Andoh ◽  
Kenji Ito ◽  
Toshiyasu Suzuki ◽  
Mitsuru Kawaguchi ◽  
...  

2021 ◽  
Vol 8 ◽  
Author(s):  
Silvia Sacchi ◽  
Valentina Rabattoni ◽  
Matteo Miceli ◽  
Loredano Pollegioni

In the central nervous system, the flavoprotein D-amino acid oxidase is responsible for catabolizing D-serine, the main endogenous coagonist of N-methyl-D-aspartate receptor. Dysregulation of D-serine brain levels in humans has been associated with neurodegenerative and psychiatric disorders. This D-amino acid is synthesized by the enzyme serine racemase, starting from the corresponding L-enantiomer, and degraded by both serine racemase (via an elimination reaction) and the flavoenzyme D-amino acid oxidase. To shed light on the role of human D-amino acid oxidase (hDAAO) in D-serine metabolism, the structural/functional relationships of this enzyme have been investigated in depth and several strategies aimed at controlling the enzymatic activity have been identified. Here, we focused on the effect of post-translational modifications: by using a combination of structural analyses, biochemical methods, and cellular studies, we investigated whether hDAAO is subjected to nitrosylation, sulfhydration, and phosphorylation. hDAAO is S-nitrosylated and this negatively affects its activity. In contrast, the hydrogen sulfide donor NaHS seems to alter the enzyme conformation, stabilizing a species with higher affinity for the flavin adenine dinucleotide cofactor and thus positively affecting enzymatic activity. Moreover, hDAAO is phosphorylated in cerebellum; however, the protein kinase involved is still unknown. Taken together, these findings indicate that D-serine levels can be also modulated by post-translational modifications of hDAAO as also known for the D-serine synthetic enzyme serine racemase.


FEBS Journal ◽  
2016 ◽  
Vol 283 (18) ◽  
pp. 3353-3370 ◽  
Author(s):  
Leila Birolo ◽  
Silvia Sacchi ◽  
Giovanni Smaldone ◽  
Gianluca Molla ◽  
Gabriella Leo ◽  
...  

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