Kinetic studies of the oxygen requirement of some amine oxidases
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Kinetic studies of the oxygen requirement of some amine oxidases by Robert Malcolm Swindell

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Published .
Written in English


  • Amine oxidase.

Book details:

Edition Notes

Other titlesOxygen requirements of some amine oxidases.
Statementby Robert Malcolm Swindell.
The Physical Object
Pagination53 leaves, bound :
Number of Pages53
ID Numbers
Open LibraryOL14326816M

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A Comparative Study of the Binding and Inhibition of Four Copper-Containing Amine Oxidases by Azide: Implications for the Role of Copper during the Oxidative Half-Reaction † Other kinetic. Cytokinin oxidase is the enzyme that catalyzes the cleavage of the N 6 side chain from adenine. The enzyme requires the δ2 double bond in the side chain for its activity. Hence, its natural substrates are isopentenyladenine and zeatin and their ribosylated derivatives (Fig. ).The enzyme is unable to cleave side chains that lack the double bond, as in dihydrozeatin and its derivatives. For some homodimeric copper amine oxidases (CuAO), there is suggestive evidence of differential activity at the two active sites implying potential cooperativity between the two monomers. Aug 15,  · Structural studies show that two tyrosyl residues ( and in human MAO B) are situated directly in front of the re faces of the covalent flavins in both MAO A and in MAO B. Aromatic residues are found in front of the flavin ring in structural studies of the amine oxidizing enzymes polyamine oxidase and trimethylamine dehydrogenase.

This experimental work tries to characterize the monoamine oxidase of microsomal origin through its kinetic and molecular properties, and to establish Cited by: Sep 05,  · Comprehension of the mechanism of oxygen reactivity in CO could, thus, shed light on the mechanisms by which flavoprotein oxidases govern the access of and the reactivity with molecular oxygen, this being a fundamental topic in biochemistry that still awaits by: described as a cytokinin oxidase. Yet, more detailed studies have revealed that the enzyme operates optimally by using quinones as electron acceptor, while the reduced enzyme reacts poorly with molecular oxygen Medium-chain acyl CoA dehydrogenase is another classic representative of flavoprotein dehydrogenases that show some sluggish activity. Oxidases catalyze the transfer of two electrons from a donor to oxygen, producing hydrogen peroxide. They usually contain flavin co-enzyme or metal in the active site to form LTQ and TPQ as a co-factor (such as the copper amine oxidases). Oxygenases catalyze the incorporation of oxygen into a substrate.

However, recent steady-state kinetic studies on the pH dependence of monoamine oxidase led to the suggestion that it is the protonated form of the amine substrate that binds to the enzyme. To investigate this further, the pH dependence of monoamine oxidase A was characterized by both steady-state and stopped-flow techniques with protiated and Cited by: Amine oxidases (AO) are enzymes widely distributed among all living organisms. 1 Their widespread occurrence accounts for an undoubtedly relevant biological function in biogenic amine metabolism. AOs represent a class of enzymes heterogenous in structure, catalytic mechanism and mode of Cited by: We are able to predict product turnover and superoxide turnover for both xanthine and lumazine using our model. The reductive rapid kinetic reaction of xanthine oxidase with lumazine has been proposed to follow a simple three step reaction sequence of substrate binding, . Jun 26,  · Studies have been made of the reaction of several carbonyl compounds with sulfite in aqueous solution. (^1)H NMR results indicate the formation of hydroxyalkanesulfonates, HXS, of general structure, RR'C(0H)(S0(_3)Na). Equilibrium and kinetic studies of the decomposition reactions have been made making use of the rapid reaction of iodine with liberated sulfite.