scholarly journals A sensitive spectrophotometric assay for peroxisomal acyl-CoA oxidase

1985 ◽  
Vol 227 (1) ◽  
pp. 205-210 ◽  
Author(s):  
G M Small ◽  
K Burdett ◽  
M J Connock
Keyword(s):  
Oxidase Activity ◽  
Mouse Liver ◽  
Enzyme Concentration ◽  
Fatty Acyl ◽  
Spectrophotometric Assay ◽  
Acid Oxidase ◽  
Rat Intestine ◽  
Amino Acid Oxidase ◽  
Acyl Coa Oxidase ◽  
First Time

A simple spectrophotometric assay was developed for peroxisomal fatty acyl-CoA oxidase activity. The assay, based on the H2O2-dependent oxidation of leuco-dichlorofluorescein catalysed by exogenous peroxidase, is more sensitive than methods previously described. By using mouse liver samples, cofactor requirements were assessed and a linear relationship was demonstrated between dye oxidation and enzyme concentration. By using this assay on subcellular fractions, palmitoyl-CoA oxidase activity was localized for the first time in microperoxisomes of rat intestine. The assay was also adapted to measure D-amino acid oxidase activity, demonstrating the versatility of this method for measuring activity of other H2O2-producing oxidases.

scholarly journals Inhibition of peroxisomal fatty acyl-CoA oxidase by antimycin A

1987 ◽  
Vol 248 (2) ◽  
pp. 603-607 ◽  
Author(s):  
J Vamecq ◽  
L Schepers ◽  
G Parmentier ◽  
G P Mannaerts
Keyword(s):  
Cellular Protein ◽  
Fatty Acyl ◽  
Acid Oxidation ◽  
Acid Oxidase ◽  
Antimycin A ◽  
Amino Acid Oxidase ◽  
Peroxisomal Fatty Acid Oxidation ◽  
Mitochondrial Monoamine Oxidase ◽  
Mitochondrial Oxidation ◽  
Acyl Coa Oxidase

Peroxisomal fatty acyl-CoA oxidase was inhibited by micromolar concentrations of antimycin A, an inhibitor of mitochondrial respiration. The inhibition was observed with all three substrates tested, i.e. palmitoyl-CoA, trihydroxycoprostanoyl-CoA and hexadecanedioyl-CoA. The peroxisomal D-amino acid oxidase was also inhibited by antimycin, but the peroxisomal L-alpha-hydroxyacid oxidase and uric acid oxidase and the mitochondrial monoamine oxidase were not. The degree of inhibition of acyl-CoA oxidase by antimycin was strongly dependent on the amount of cellular protein present in the assay mixture: at a fixed antimycin concentration, the inhibition was gradually lost with increasing protein concentrations. At a fixed cellular protein concentration in the assay mixtures, the mitochondrial oxidation of glutamate or palmitoylcarnitine was inhibited at antimycin concentrations that were much lower than those required for the inhibition of fatty acyl-CoA oxidase. Our results, nevertheless, demonstrate that antimycin A must be used with caution, when it is added to homogenates or subcellular fractions in order to distinguish between mitochondrial and peroxisomal fatty acid oxidation.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

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.

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

Science ◽  
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

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

1991 ◽  
Vol 23 (11) ◽  
pp. 1301-1305 ◽  
Author(s):  
Konno Ryuichi ◽  
Yamamoto Katsuhiko ◽  
Niwa Akira ◽  
Yasumura Yosihiro
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Mutant Mice ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

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.

A single-base-pair substitution abolishes d-amino-acid oxidase activity in the mouse

1992 ◽  
Vol 1139 (4) ◽  
pp. 315-318 ◽  
Author(s):  
Masato Sasaki ◽  
Ryuichi Konno ◽  
Masahiro Nihio ◽  
Akira Niwa ◽  
Yosihiro Yasumura ◽  
...  
Keyword(s):  
Amino Acid ◽  
Base Pair ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Single Base ◽  
Single Base Pair Substitution ◽  
Single Base Pair ◽  
Base Pair Substitution

Determination of Free -Proline and -Leucine in the Brains of Mutant Mice Lacking -Amino Acid Oxidase Activity

2001 ◽  
Vol 298 (2) ◽  
pp. 253-258 ◽  
Author(s):  
Kenji Hamase ◽  
Tomomi Inoue ◽  
Akiko Morikawa ◽  
Ryuichi Konno ◽  
Kiyoshi Zaitsu
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Mutant Mice ◽  
Acid Oxidase ◽  
Free Proline ◽  
Amino Acid Oxidase

scholarly journals Genetic loss of D-amino acid oxidase activity reverses schizophrenia-like phenotypes in mice

2010 ◽  
Vol 9 (1) ◽  
pp. 11-25 ◽  
Author(s):  
V. Labrie ◽  
W. Wang ◽  
S. W. Barger ◽  
G. B. Baker ◽  
J. C. Roder
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase
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