Specific immobilization of d-amino acid oxidase on hematin-functionalized support mimicking multi-enzyme catalysis

2015 ◽  
Vol 17 (8) ◽  
pp. 4465-4472 ◽  
Author(s):  
Jian Sun ◽  
Kun Du ◽  
Xiaoqiang Song ◽  
Qian Gao ◽  
Hao Wu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Specifically immobilized enzyme and hematin sequentially catalyze the conversion of d-alanine and the decomposition of the generated hydrogen peroxide.

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.

Effect of hydrogen peroxide on d-amino acid oxidase from Rhodotorula gracilis

2000 ◽  
Vol 27 (3-5) ◽  
pp. 234-239 ◽  
Author(s):  
Isabel de la Mata ◽  
Fernando Ramón ◽  
Virginia Obregón ◽  
Ma Pilar Castillón ◽  
Carmen Acebal
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

Nitroalkanes as Reductive Substrates for Flavoprotein Oxidases

1972 ◽  
Vol 27 (9) ◽  
pp. 1052-1053 ◽  
Author(s):  
David J. T. Porter ◽  
Judith G. Voet ◽  
Harold J. Bright
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Glucose Oxidase ◽  
Ph Dependence ◽  
Kinetic Mechanism ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Kinetics Of ◽  
Oxidase Reaction ◽  
Detailed Kinetic Mechanism

Nitroalkanes have been found to be general reductive substrates for D-amino acid oxidase, glucose oxidase and L-amino acid oxidase. These enzymes show different specificities for the structure of the nitroalkane substrate.The stoichiometry of the D-amino acid oxidase reaction is straightforward, consisting of the production of one mole each of aldehyde, nitrite and hydrogen peroxide for each mole of nitroalkane and oxygen consumed. The stoichiometry of the glucose oxidase reaction is more complex in that less than one mole of hydrogen peroxide and nitrite is produced and nitrate and traces of 1-dinitroalkane are formed.The kinetics of nitroalkane oxidation show that the nitroalkane anion is much more reactive in reducing the flavin than is the neutral substrate. The pH dependence of flavin reduction strongly suggests that proton abstraction is a necessary event in catalysis. A detailed kinetic mechanism is presented for the oxidation of nitroethane by glucose.It has been possible to trap a form of modified flavin in the reaction of D-amino acid oxidase with nitromethane from which oxidized FAD can be regenerated in aqueous solution in the presence of oxygen.

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.

scholarly journals Uricase, amino acid oxidase, and xanthine oxidase

1936 ◽  
Vol 119 (813) ◽  
pp. 114-140 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Amino Acid ◽  
Xanthine Oxidase ◽  
Pure Oxygen ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Unstable Compound ◽  
The Comparative Study ◽  
The Relationship

The object of this paper is the comparative study of three oxidizing enzymes—uricase, amino acid oxidase, and xanthine oxidase. We shall describe first the main properties of uricase and amino acid oxidase, laying special stress on characters which have not been sufficiently investigated by previous workers. This will include the study of the effect of various factors on the activity of these enzymes, the reaction between these enzymes and their substrates, the activation of the substrate molecules, their reaction with the molecular oxygen, and the reduction of the latter to hydrogen peroxide. We shall then examine briefly the main characters of xanthine oxidase, and this will enable us to compare the properties of these three enzymes and to determine some of the characters they have in common. II−Uricase or Urico-oxidase 1− Previous Work That uricase or urico-oxidase catalyses the oxidation of uric acid to allantoin has been known since the work of Schittenhelm (1905), Wiechowski and Wiener (1909), and others, but its main properties have been established only by Battelli and Stern (1909, 1912) in their important investigation on this subject. According to these authors, for the oxidation of a molecule of uric acid to allantoin one atom of oxygen and one molecule of water are taken up while one molecule of CO 2 is given off. The reaction consists, therefore, in oxidation, hydration, and decarboxylation, and the R. Q. of the reaction is usually equal to 2. It varies slightly, however, according to the age of the enzyme preparation. The relationship which these authors have established between the amount of uric acid disappearing, the oxygen taken up, and the CO 2 given off, has made possible the study of the reaction by the estimation of either oxygen or CO 2 . The velocity of oxidation of uric acid was found to depend on the oxygen tension, being, for instance, at least twice as great in pure oxygen as in air. The main results obtained by Battelli and Stern have been recently confirmed by other workers, who have, however, paid special attention to the study of the kinetics of this reaction (Felix, Scheel, and Schuler, 1929; Schuler, 1932; Rô, 1931; Grynberg, 1931). The velocity of the reaction was measured by these authors in terms of the amount of uric acid oxidized, of oxygen absorbed, and of CO 2 liberated; and these reactions were studied at various hydrogen ion concentrations, at different tensions of oxygen, and at different concentrations of enzyme and substrate. The oxidation of uric acid catalysed by the enzyme was also compared with that obtained by permanganate and by hydrogen peroxide. One of the important conclusions which resulted from this work was that the enzyme does not catalyse directly the oxidation of uric acid to allantoin, but that the reaction takes place in two steps: (1) the catalytic oxidation and hydration of uric acid by uricase to an oxyacetylene-diurein carboxylic acid, and (2) the decarboxylation of this unstable compound to allantoin, which is independent of the enzyme (Biltz and Schauder, 1923; Felix and his co-workers, 1929; Grynberg, 1931; and Schuler, 1932).

Electroanalysis of D-Amino Acid Oxidase and Its Interaction with Hydrogen Peroxide

2008 ◽  
Vol 41 (8) ◽  
pp. 1408-1418 ◽  
Author(s):  
Nandi Zhou ◽  
Zhenyu Shao ◽  
Yinxi Huang ◽  
Tongyang Zhu ◽  
Genxi Li
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase
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