scholarly journals Oxidation and enzyme-activated irreversible inhibition of rat liver monoamine oxidase-B by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

1986 ◽  
Vol 240 (2) ◽  
pp. 379-383 ◽  
Author(s):  
K F Tipton ◽  
J M McCrodden ◽  
M B Youdim
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Maximum Velocity ◽  
Monoamine Oxidase B ◽  
Half Time ◽  
Inhibitory Process ◽  
Irreversible Inhibitor ◽  
Irreversible Inhibition ◽  
Km Value ◽  
Lower Maximum

The compound 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), which produces symptoms resembling Parkinson's disease in humans, acts both as a substrate and an enzyme-activated irreversible inhibitor of the B-form of monoamine oxidase from rat liver. Analysis of the inhibitory process showed the compound to be considerably more efficient as a substrate than as an irreversible inhibitor, with about 17000 mol of product being formed per mol of enzyme inactivated. The half-time of the inhibitory process was about 22 min. With the A-form of the enzyme, the compound had a lower Km value and a considerably lower maximum velocity than the corresponding values obtained with the B-form. Under the conditions used in the present work the inhibition of the A-form of the enzyme was largely reversible.

scholarly journals A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes

1974 ◽  
Vol 139 (3) ◽  
pp. 645-652 ◽  
Author(s):  
Miles D. Houslay ◽  
Keith F. Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Monoamine Oxidase Activity ◽  
Irreversible Inhibitor ◽  
Kinetic Evaluation ◽  
Reversible Inhibitors ◽  
Substrate Specificities ◽  
Outer Membranes ◽  
Enzyme Species

1. A preparation of mitochondrial outer membranes from rat liver can be shown to contain two kinetically distinct monoamine oxidase activities. These activities are distinguishable by their different sensitivities to the irreversible inhibitor clorgyline, and by the effect of the reversible inhibitors benzyl cyanide and 4-cyanophenol. 2. The substrate specificities of the preparation and the two enzyme species have been elucidated.

Irreversible Inhibition of Monoamine Oxidase B by the Antiparkinsonian Medicines Rasagiline and Selegiline: A Computational Study

2011 ◽  
Vol 2011 (32) ◽  
pp. 6419-6433 ◽  
Author(s):  
Rok Borštnar ◽  
Matej Repič ◽  
Mojca Kržan ◽  
Janez Mavri ◽  
Robert Vianello
Keyword(s):  
Monoamine Oxidase ◽  
Computational Study ◽  
Monoamine Oxidase B ◽  
Irreversible Inhibition

scholarly journals Mechanism-based inhibition of monoamine oxidase by 3-aryl-Δ3-pyrrolines

1998 ◽  
Vol 336 (1) ◽  
pp. 63-67 ◽  
Author(s):  
Carvell H. WILLIAMS ◽  
Jill LAWSON
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Monoamine Oxidase B ◽  
Step Process ◽  
Mao B ◽  
Enzymic Oxidation ◽  
Irreversible Inhibitors ◽  
Inhibition Process

The compound 1-methyl-3-phenyl-Δ3-pyrroline and its 4-chlorophenyl analogue appear to act as irreversible inhibitors of monoamine oxidase B (MAO B) in mitochondria of rat liver. The compounds are metabolized by MAO B and concomitantly inhibit the enzyme in what seems to be a two-step process. The metabolic end product of this process is the corresponding pyrrole. This inhibition process is considered in the light of possible intermediates formed during the enzymic oxidation, and comparisons are made with the structurally analogous neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine.

Molecular cloning of a cDNA for rat liver monoamine oxidase B

1988 ◽  
Vol 157 (3) ◽  
pp. 970-976 ◽  
Author(s):  
Akio Ito ◽  
Toyoko Kuwahara ◽  
Shuichiro Inadome ◽  
Yasuhiro Sagara
Keyword(s):  
Monoamine Oxidase ◽  
Molecular Cloning ◽  
Rat Liver ◽  
Monoamine Oxidase B
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