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
ChemInform ◽  
2010 ◽  
Vol 27 (6) ◽  
pp. no-no
Author(s):  
J. C. G. WOO ◽  
X. WANG ◽  
R. B. SILVERMAN

2020 ◽  
Author(s):  
Ashley P. Mattey ◽  
Jack J. sangster ◽  
Christopher Baldwin ◽  
Jeremy I. Ramsden ◽  
William R. Birmingham ◽  
...  

Characterisation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals is described. Engineered galactose oxidase (GOase) variants M1 and M3-5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on solid support, outperforming their free counterparts in terms of stability, resistance to heat, and tolerance to neat organic solvents. While immobilisation of oxidase biocatalysts improves properties that are critical for industrial implementation, they additionally showed versatility as the biocatalyst batches can be recovered, washed and reused multiple times for the oxidation of different substrates.


1986 ◽  
Vol 102 (6) ◽  
pp. 1675-1677
Author(s):  
O. �. Volkovitskaya ◽  
P. G. Bochev ◽  
S. R. Ribarov ◽  
V. Z. Gorkin ◽  
V. E. Kagan

1980 ◽  
Vol 102 (23) ◽  
pp. 7126-7128 ◽  
Author(s):  
Richard B. Silverman ◽  
Stephen J. Hoffman ◽  
William B. Catus

2020 ◽  
Author(s):  
Ashley P. Mattey ◽  
Jack J. sangster ◽  
Christopher Baldwin ◽  
Jeremy I. Ramsden ◽  
William R. Birmingham ◽  
...  

Characterisation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals is described. Engineered galactose oxidase (GOase) variants M1 and M3-5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on solid support, outperforming their free counterparts in terms of stability, resistance to heat, and tolerance to neat organic solvents. While immobilisation of oxidase biocatalysts improves properties that are critical for industrial implementation, they additionally showed versatility as the biocatalyst batches can be recovered, washed and reused multiple times for the oxidation of different substrates.


Medicines ◽  
2020 ◽  
Vol 7 (4) ◽  
pp. 18
Author(s):  
Wiem Haj Ahmed ◽  
Cécile Peiro ◽  
Jessica Fontaine ◽  
Barry J. Ryan ◽  
Gemma K. Kinsella ◽  
...  

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.


2015 ◽  
Vol 127 (31) ◽  
pp. 9125-9128 ◽  
Author(s):  
Alexander T. Murray ◽  
Myles J. H. Dowley ◽  
Fabienne Pradaux-Caggiano ◽  
Amgalanbaatar Baldansuren ◽  
Alistair J. Fielding ◽  
...  

2015 ◽  
Vol 54 (31) ◽  
pp. 8997-9000 ◽  
Author(s):  
Alexander T. Murray ◽  
Myles J. H. Dowley ◽  
Fabienne Pradaux-Caggiano ◽  
Amgalanbaatar Baldansuren ◽  
Alistair J. Fielding ◽  
...  

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