Summary
Monoamine oxidase (MAO) A and B have selective substrate and inhibitor specificity. MAO A and B knock-out mice exhibit distinct neurotransmitter metabolism and behavior, suggesting that these two isoenzymes have distinct functions in vivo. These two isoenzymes are coded by different cDNAs with 70% amino acid identity. Interestingly, Isoleucine 335 in MAO A and the corresponding amino acid in MAO B, tyrosine 326, determine the substrate and inhibitor selectivity in vitro.
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Shih, J.C., Chen, K. (2002). In Vivo and in Vitro Functions of Two Types of Mao. In: Nagatsu, T., Nabeshima, T., McCarty, R., Goldstein, D.S. (eds) Catecholamine Research. Advances in Behavioral Biology, vol 53. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-3538-3_32
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DOI: https://doi.org/10.1007/978-1-4757-3538-3_32
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