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Determination of regions important for Monoamine Oxidase (MAO) A and B substrate and inhibitor selectivities

  • J. C. Shih
  • K. Chen
  • R. M. Geha
Part of the Journal of Neural Transmission. Supplement book series (NEURAL SUPPL, volume 52)

Summary

MAO-A and -B are defined by their substrate and inhibitor preferences. To determine which regions of the isoenzymes confer these preferences, we have constructed six chimeric MAO enzymes by reciprocally exchanging corresponding N-terminal, C-terminal, and internal segments of MAO-A and -B then determined the catalytic properties of these chimeric enzymes. N-terminal chimerics A45B and B36A were made by exchanging amino acid segments 1–45 and 1–36 of MAO-A and -B respectively. Cterminal chimerics A402B and B393A were made by exchanging amino acid segments 403-527 and 394-520 of MAO-A and -B respectively, and internal chimerics AB161_375A and BA152–366B were made by exchanging amino acid segments 161–375 and 152–366 of MAO-A and -B respectively. The enzymatic properties observed for the chimerics suggest that the exchanged internal regions but not the N- or C-terminal regions confer substrate and inhibitor preferences.

The enzymatic properties observed for the chimerics suggest that the exchanged internal regions but not the N- or C-terminal regions confer substrate and inhibitor preferences.

Keywords

Monoamine Oxidase Enzymatic Property Exchange Amino Acid Internal Segment Chimeric Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag Wien 1998

Authors and Affiliations

  • J. C. Shih
    • 1
  • K. Chen
    • 1
  • R. M. Geha
    • 1
  1. 1.Department of Molecular Pharmacology and Toxicology, School of PharmacyUniversity of Southern CaliforniaLos AngelesUSA

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