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Author Notes:

Correspondence: Roberto Orru, Department of Biochemistry, Emory University, Rollins Research Center, 1510 Clifton Road, Atlanta, Georgia 30322 USA; Email: rorru@emory.edu.

Subjects:

Research Funding:

This work was supported by a grant from the National Institutes of Health (GM29433).

Keywords:

  • monoamine oxidase A
  • monoamine oxidase B
  • human
  • mechanistic properties

Do MAO A and MAO B utilize the same mechanism for the C-H bond cleavage step in catalysis? Evidence suggesting differing mechanisms

Tools:

Journal Title:

Journal of Neural Transmission

Volume:

Volume 120, Number 6

Publisher:

, Pages 847-851

Type of Work:

Article | Post-print: After Peer Review

Abstract:

Summary The detailed molecular mechanism proposed for the MAO-catalyzed oxidation of amines has been controversial with the basic assumption that both MAO A and MAO B follow the same pathway for the C-H bond cleavage step. Using the mechanistic approach of investigation of electronic effects of various benzylamine ring substituents in experiments at pH=9.0, human MAO A exhibits a kinetic behavior characteristic of a H+ abstraction while human MAO B exhibits kinetic properties characteristic of a H− abstraction. These results lead to the conclusion that the assumption that MAO A and MAO B follow identical mechanisms is incorrect.

Copyright information:

Springer-Verlag Wien 2013

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