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

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.

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References

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Authors and Affiliations

1. Department of Molecular Pharmacology and Toxicology, School of Pharmacy, University of Southern California, 1985 Zonal Avenue, Los Angeles, CA, USA
   J. C. Shih Ph.D., K. Chen & R. M. Geha

Authors

1. J. C. Shih Ph.D.
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2. K. Chen
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3. R. M. Geha
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Editors and Affiliations

1. Department of Pharmacology, The Bruce Rappaport Faculty of Medicine, Technion — Israel Institute of Technology, Haifa, Israel
   J. P. M. Finberg & M. B. H. Youdim &
2. Clinical Neurochemistry, Department of Psychiatry, University of Würzburg, Federal Republic of Germany
   P. Riederer
3. Biochemistry Department, Trinity College, Dublin, Ireland
   K. F. Tipton

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© 1998 Springer-Verlag Wien

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Shih, J.C., Chen, K., Geha, R.M. (1998). Determination of regions important for Monoamine Oxidase (MAO) A and B substrate and inhibitor selectivities. In: Finberg, J.P.M., Youdim, M.B.H., Riederer, P., Tipton, K.F. (eds) MAO — The Mother of all Amine Oxidases. Journal of Neural Transmission. Supplement, vol 52. Springer, Vienna. https://doi.org/10.1007/978-3-7091-6499-0\_1

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• DOI: https://doi.org/10.1007/978-3-7091-6499-0\_1
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• Print ISBN: 978-3-211-83037-6
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