scholarly journals Role of d -amino acid oxidase in the production of kynurenine pathway metabolites from d -tryptophan in mice

2016 ◽  
Vol 136 (4) ◽  
pp. 804-814 ◽  
Author(s):  
Francesca M. Notarangelo ◽  
Xiao-Dan Wang ◽  
Kyle J. Horning ◽  
Robert Schwarcz
Keyword(s):  
Amino Acid ◽  
Kynurenine Pathway ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids.

1993 ◽  
Vol 268 (36) ◽  
pp. 26941-26949
Author(s):  
A D'Aniello ◽  
G D'Onofrio ◽  
M Pischetola ◽  
G D'Aniello ◽  
A Vetere ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Biological Role ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Questioning on the role of D amino acid oxidase in familial amyotrophic lateral sclerosis

2010 ◽  
Vol 107 (26) ◽  
pp. E107-E107 ◽  
Author(s):  
S. Millecamps ◽  
S. Da Barroca ◽  
C. Cazeneuve ◽  
F. Salachas ◽  
P.-F. Pradat ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Amino Acid ◽  
Familial Amyotrophic Lateral Sclerosis ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Lateral Sclerosis

scholarly journals Role of l-amino acid oxidase isolated from Calloselasma rhodostoma venom on neutrophil NADPH oxidase complex activation

Toxicon ◽  
2018 ◽  
Vol 145 ◽  
pp. 48-55 ◽  
Author(s):  
Mauro Valentino Paloschi ◽  
Charles Nunes Boeno ◽  
Jéssica Amaral Lopes ◽  
André Eduardo dos Santos da Rosa ◽  
Weverson Luciano Pires ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nadph Oxidase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Nadph Oxidase Complex ◽  
Calloselasma Rhodostoma

D-Serine metabolism: new insights into the modulation of D-amino acid oxidase activity

2013 ◽  
Vol 41 (6) ◽  
pp. 1551-1556 ◽  
Author(s):  
Silvia Sacchi
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Endogenous Ligand ◽  
Amino Acid Oxidase ◽  
The Brain ◽  
Serine Metabolism ◽  
Synthesis And Degradation

Over the years, accumulating evidence has indicated that D-serine represents the main endogenous ligand of NMDA (N-methyl-D-aspartate) receptors. In the brain, the concentration of D-serine stored in cells is defined by the activity of two enzymes: serine racemase (responsible for both the synthesis and degradation) and D-amino acid oxidase (which catalyses D-serine degradation). The present review is focused on human D-amino acid oxidase, discussing the mechanisms involved in modulating enzyme activity and stability, with the aim to substantiate the pivotal role of D-amino acid oxidase in brain D-serine metabolism.

The formation of choleglobin and the role of catalase in the erythrocyte

1949 ◽  
Vol 136 (884) ◽  
pp. 435-448 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Catalase Activity ◽  
Acid Oxidase ◽  
Small Decrease ◽  
Amino Acid Oxidase ◽  
Oxidase System ◽  
Inverse Proportion

In haemolysates of non-nucleated erythrocytes there is an inverse proportion between catalase activity and rate of choleglobin formation on addition of ascorbic acid. In the intact erythrocytes catalase protects haemoglobin against oxidation and further destruction by the hydrogen peroxide generated by the D-amino-acid oxidase system or by physiological concentrations of ascorbic acid and glutathione. Acid destromatization of haemolyzed horse erythrocytes causes a small decrease in the catalase activity and an increased rate of inactivation of the remaining catalase by ascorbic acid. The liberation of copper from haemocuprein is quantitatively insufficient to explain the decreased stability of the catalase. Exposing duck oxyhaemoglobin, but not reduced haemoglobin, to a pH of 5⋅5 to 5⋅8, causes an alteration which is apparent from the increase of the rate of choleglobin formation. The mechanism of this alteration is discussed. It partly explains the 'stroma effect', at least in duck erythrocytes. In addition, in the latter, there is a true stroma effect. Choleglobin formation in the presence of ascorbic acid is accelerated by a variety of substances. Some of these perturb haemoglobin, while others increase the formation of hydrogen peroxide from ascorbic acid. The implications of our findings on the mechanism of choleglobin formation and on the role of catalase in the erythrocyte are discussed.

Indispensable but Insufficient Role of Renal D-Amino Acid Oxidase in Chiral Inversion of NG-Nitro-D-arginine

2010 ◽  
Vol 7 (6) ◽  
pp. 1413-1423 ◽  
Author(s):  
Yan-Fei Xin ◽  
Xin Li ◽  
Bin Hao ◽  
Nian Gong ◽  
Wen-Qiang Sun ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Chiral Inversion ◽  
Amino Acid Oxidase

scholarly journals Studies on the structural and functional aspects of Rhodotorula gracilisd-amino acid oxidase by limited trypsinolysis

1995 ◽  
Vol 310 (2) ◽  
pp. 577-583 ◽  
Author(s):  
L Pollegioni ◽  
F Ceciliani ◽  
B Curti ◽  
S Ronchi ◽  
M S Pilone
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Compact Structure ◽  
Peptide Bonds ◽  
Functional Aspects ◽  
Complex Forms ◽  
Limited Trypsinolysis ◽  
Dimerization Process

The structure-function relationships of purified Rhodotorula gracilis D-amino acid oxidase (in its holo-, apo- and holo-enzyme-benzoate complex forms) was analysed by digestion with trypsin. In all cases trypsin cleaves this 80 kDa dimeric enzyme at the C-terminal region, since the peptide bonds sensitive to proteinase attack are clustered in this region. Digestion of native enzyme with trypsin produced a nicked and truncated form of 38.3 kDa containing two polypeptides of 34 and 5 kDa starting from Met1 and Ala319 respectively, and with detachment of the Thr306-Arg318 and Glu365-Leu368 peptides. Our results show that this *#x2018;core’, folded into a compact structure, is catalytically competent. The acquisition of this nicked form was marked by a shift from a dimeric to a monomeric active enzyme, a result never previously obtained. The deleted sequences, Thr306-Arg318 and Glu365-Leu368, are essential for the monomer-monomer interaction, and, in particular, the region encompassing Thr306-Arg318 should play an essential role in the dimerization process. interestingly, the Ser308-Lys321 sequence present in the lost peptide corresponds to a sequence not present in other known D-amino acid oxidases [Faotto, Pollegioni, Ceciliani, Ronchi and Pilone (1995) Biotechnol. Lett. 17, 193-198]. A role of the cleaved-off region for the thermostabilization of the enzyme is also discussed.

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