Identification of the Active Site Cysteine in Bovine Liver Monoamine Oxidase B

1997 ◽  
Vol 119 (28) ◽  
pp. 6690-6691 ◽  
Author(s):  
Boyu Zhong ◽  
Richard B. Silverman
Keyword(s):  
Monoamine Oxidase ◽  
Active Site ◽  
Bovine Liver ◽  
Monoamine Oxidase B ◽  
Active Site Cysteine

scholarly journals Oxidation of 3-amino-1-phenylprop-1-enes by monoamine oxidase and their use in a continuous assay of the enzyme

1988 ◽  
Vol 256 (3) ◽  
pp. 911-915 ◽  
Author(s):  
C H Williams ◽  
J Lawson ◽  
F R C Backwell
Keyword(s):  
Monoamine Oxidase ◽  
Absorption Coefficient ◽  
Mitochondrial Protein ◽  
Bovine Liver ◽  
Spectrophotometric Assay ◽  
Monoamine Oxidase A ◽  
Monoamine Oxidase B ◽  
High Absorption Coefficient ◽  
Continuous Assay ◽  
High Absorption

3-Amino-1-phenylprop-1-ene (cinnamylamine) and some derivatives were examined as substrates for monoamine oxidases A and B in mitochondria. All of the amines examined were readily oxidized by monoamine oxidase B but much less readily by monoamine oxidase A. E-Cinnamylamine was found to have Km 0.025 mM and Vmax. 3.9 nmol/min per mg of mitochondrial protein. Corresponding values with monoamine oxidase A were 0.026 mM and 0.85 nmol/min per mg respectively. Despite their different stereochemistry, E- and Z-N-methylcinnamylamines were almost equally effective as substrates for monoamine oxidase B. The characteristic u.v. absorbance and high absorption coefficient of cinnamaldehyde, the product produced by enzymic oxidation of cinnamylamine, is utilized in a sensitive continuous spectrophotometric assay for both enzymes in the rat and for the assay of a purified monoamine oxidase B from bovine liver.

scholarly journals Why does the Y326I mutant of monoamine oxidase B decompose an endogenous amphetamine at a slower rate than the wild type enzyme? Reaction step elucidated by multiscale molecular simulations

2018 ◽  
Vol 20 (6) ◽  
pp. 4181-4188 ◽  
Author(s):  
Domen Pregeljc ◽  
Urška Jug ◽  
Janez Mavri ◽  
Jernej Stare
Keyword(s):  
Monoamine Oxidase ◽  
Active Site ◽  
Molecular Simulations ◽  
Enzyme Reaction ◽  
Monoamine Oxidase B ◽  
Wild Type ◽  
Reaction Step ◽  
Wild Type Enzyme ◽  
Mao B

Mutated MAO B enzyme decomposes phenylethylamine at slower rate due to changed interactions in the active site.

scholarly journals Computational Study of the pKa Values of Potential Catalytic Residues in the Active Site of Monoamine Oxidase B

2012 ◽  
Vol 8 (10) ◽  
pp. 3864-3870 ◽  
Author(s):  
Rok Borštnar ◽  
Matej Repič ◽  
Shina Caroline Lynn Kamerlin ◽  
Robert Vianello ◽  
Janez Mavri
Keyword(s):  
Monoamine Oxidase ◽  
Active Site ◽  
Computational Study ◽  
Monoamine Oxidase B ◽  
Pka Values ◽  
Catalytic Residues
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