Study on the decrease of renal d-amino acid oxidase activity in the rat after renal ischemia by chiral ligand exchange capillary electrophoresis

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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The Effect of Castration and Testosterone Propionate on d-Amino Acid Oxidase Activity in the Mouse

Science ◽

10.1126/science.98.2534.89.a ◽

1943 ◽

Vol 98 (2534) ◽

pp. 89-89

Author(s):

L. C. Clark ◽

C. D. Kochakian ◽

R. Phyllis Fox

Keyword(s):

Amino Acid ◽

Oxidase Activity ◽

Testosterone Propionate ◽

Acid Oxidase ◽

Amino Acid Oxidase

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Presence of d-amino-acid oxidase protein in mutant mice lacking d-amino-acid oxidase activity

International Journal of Biochemistry ◽

10.1016/0020-711x(91)90231-b ◽

1991 ◽

Vol 23 (11) ◽

pp. 1301-1305 ◽

Cited By ~ 9

Author(s):

Konno Ryuichi ◽

Yamamoto Katsuhiko ◽

Niwa Akira ◽

Yasumura Yosihiro

Keyword(s):

Amino Acid ◽

Oxidase Activity ◽

Mutant Mice ◽

Acid Oxidase ◽

Amino Acid Oxidase

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

Biochemical Society Transactions ◽

10.1042/bst20130184 ◽

2013 ◽

Vol 41 (6) ◽

pp. 1551-1556 ◽

Cited By ~ 10

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.

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