Evidence against a Nucleophilic Mechanism for Monoamine Oxidase-Catalyzed Amine Oxidation

1994 ◽  
Vol 116 (9) ◽  
pp. 4129-4130 ◽  
Author(s):  
Richard B. Silverman ◽  
Xingliang Lu
Keyword(s):  
Monoamine Oxidase ◽  
Amine Oxidation ◽  
Nucleophilic Mechanism

Monoamine Oxidase B-Catalyzed Oxidation of Cinnamylamine 2,3-Oxide. Further Evidence against a Nucleophilic Mechanism

1994 ◽  
Vol 116 (25) ◽  
pp. 11590-11591 ◽  
Author(s):  
Richard B. Silverman ◽  
Xingliang Lu ◽  
Joseph J. P. Zhou ◽  
Aaron Swihart
Keyword(s):  
Monoamine Oxidase ◽  
Monoamine Oxidase B ◽  
Nucleophilic Mechanism ◽  
Catalyzed Oxidation

Monoamine oxidase-catalyzed amine oxidation in organic solvents

1995 ◽  
Vol 60 (19) ◽  
pp. 6235-6236 ◽  
Author(s):  
Jonathan C. G. Woo ◽  
Xueqing Wang ◽  
Richard B. Silverman
Keyword(s):  
Monoamine Oxidase ◽  
Organic Solvents ◽  
Amine Oxidation

Superoxide radical generation during biogenic amine oxidation catalyzed by mitochondrial monoamine oxidase

1986 ◽  
Vol 102 (6) ◽  
pp. 1675-1677
Author(s):  
O. �. Volkovitskaya ◽  
P. G. Bochev ◽  
S. R. Ribarov ◽  
V. Z. Gorkin ◽  
V. E. Kagan
Keyword(s):  
Monoamine Oxidase ◽  
Biogenic Amine ◽  
Superoxide Radical ◽  
Amine Oxidation ◽  
Mitochondrial Monoamine Oxidase ◽  
Radical Generation

A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation

1980 ◽  
Vol 102 (23) ◽  
pp. 7126-7128 ◽  
Author(s):  
Richard B. Silverman ◽  
Stephen J. Hoffman ◽  
William B. Catus
Keyword(s):  
Monoamine Oxidase ◽  
Amine Oxidation ◽  
Mitochondrial Monoamine Oxidase

scholarly journals Methylxanthines Inhibit Primary Amine Oxidase and Monoamine Oxidase Activities of Human Adipose Tissue

Medicines ◽  
2020 ◽  
Vol 7 (4) ◽  
pp. 18
Author(s):  
Wiem Haj Ahmed ◽  
Cécile Peiro ◽  
Jessica Fontaine ◽  
Barry J. Ryan ◽  
Gemma K. Kinsella ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Monoamine Oxidase ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Fluorimetric Determination ◽  
Amine Oxidation ◽  
Direct Demonstration ◽  
Primary Amine Oxidase ◽  
Anti Inflammatory ◽  
Subcutaneous Adipose

Background: Methylxanthines including caffeine and theobromine are widely consumed compounds and were recently shown to interact with bovine copper-containing amine oxidase. To the best of our knowledge, no direct demonstration of any interplay between these phytochemicals and human primary amine oxidase (PrAO) has been reported to date. We took advantage of the coexistence of PrAO and monoamine oxidase (MAO) activities in human subcutaneous adipose tissue (hScAT) to test the interaction between several methylxanthines and these enzymes, which are involved in many key pathophysiological processes. Methods: Benzylamine, methylamine, and tyramine were used as substrates for PrAO and MAO in homogenates of subcutaneous adipose depots obtained from overweight women undergoing plastic surgery. Methylxanthines were tested as substrates or inhibitors by fluorimetric determination of hydrogen peroxide, an end-product of amine oxidation. Results: Semicarbazide-sensitive PrAO activity was inhibited by theobromine, caffeine, and isobutylmethylxanthine (IBMX) while theophylline, paraxanthine, and 7-methylxanthine had little effect. Theobromine inhibited PrAO activity by 54% at 2.5 mM. Overall, the relationship between methylxanthine structure and the degree of inhibition was similar to that seen with bovine PrAO, although higher concentrations (mM) were required for inhibition. Theobromine also inhibited oxidation of tyramine by MAO, at the limits of its solubility in a DMSO vehicle. At doses higher than 12 % v/v, DMSO impaired MAO activity. MAO was also inhibited by millimolar doses of IBMX, caffeine and by other methylxanthines to a lesser extent. Conclusions: This preclinical study extrapolates previous findings with bovine PrAO to human tissues. Given that PrAO is a potential target for anti-inflammatory drugs, it indicates that alongside phosphodiesterase inhibition and adenosine receptor antagonism, PrAO and MAO inhibition could contribute to the health benefits of methylxanthines, especially their anti-inflammatory effects.

scholarly journals Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B

2015 ◽  
Vol 127 (31) ◽  
pp. 9125-9128 ◽  
Author(s):  
Alexander T. Murray ◽  
Myles J. H. Dowley ◽  
Fabienne Pradaux-Caggiano ◽  
Amgalanbaatar Baldansuren ◽  
Alistair J. Fielding ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Monoamine Oxidase B ◽  
Aerobic Conditions ◽  
Amine Oxidation

scholarly journals Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B

2015 ◽  
Vol 54 (31) ◽  
pp. 8997-9000 ◽  
Author(s):  
Alexander T. Murray ◽  
Myles J. H. Dowley ◽  
Fabienne Pradaux-Caggiano ◽  
Amgalanbaatar Baldansuren ◽  
Alistair J. Fielding ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Monoamine Oxidase B ◽  
Aerobic Conditions ◽  
Amine Oxidation

ChemInform Abstract: Monoamine Oxidase-Catalyzed Amine Oxidation in Organic Solvents.

ChemInform ◽  
2010 ◽  
Vol 27 (6) ◽  
pp. no-no
Author(s):  
J. C. G. WOO ◽  
X. WANG ◽  
R. B. SILVERMAN
Keyword(s):  
Monoamine Oxidase ◽  
Organic Solvents ◽  
Amine Oxidation

Neuronal and Extraneuronal Uptake of 3H-Norepinephrine in the Heart of the Active Bat: An Electron Microscopic Radioautographic Study

1973 ◽  
Vol 31 ◽  
pp. 522-523
Author(s):  
Martin Hagopian ◽  
Michael D. Gershon ◽  
Eladio A. Nunez
Keyword(s):  
Smooth Muscle ◽  
Monoamine Oxidase ◽  
Vascular Smooth Muscle ◽  
Cardiac Muscle ◽  
Maximum Rate ◽  
External Medium ◽  
Extraneuronal Uptake ◽  
Electron Microscopic ◽  
Cardiac Tissues ◽  
High Affinity

The ability of cardiac tissues to take up norepinephrine from an external medium is well known. Two mechanisms, called Uptake and Uptake respectively by Iversen have been differentiated. Uptake is a high affinity system associated with adrenergic neuronal elements. Uptake is a low affinity system, with a higher maximum rate than that of Uptake. Uptake has been associated with extraneuronal tissues such as cardiac muscle, fibroblasts or vascular smooth muscle. At low perfusion concentrations of norepinephrine most of the amine taken up by Uptake is metabolized. In order to study the localization of sites of norepinephrine storage following its uptake in the active bat heart, tritiated norepinephrine (2.5 mCi; 0.064 mg) was given intravenously to 2 bats. Monoamine oxidase had been inhibited with pheniprazine (10 mg/kg) one hour previously to decrease metabolism of norepinephrine.

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