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(Received for publication, March 27, 1997, and in revised form, April 9, 1997)
From the Department of Chemistry, Faculty of Science, Kyushu
University, Fukuoka 812-81, Japan
Monoamine oxidase (MAO) oxidizes biologically
important amines including neurotransmitters and plays a central role
in the regulation of intracellular level of these amines. Two distinct forms of MAO (MAO A and MAO B) were defined based on differences in
substrate and inhibitor specificities. We earlier reported that the
region between about residues 120 and 220 of rat MAO is responsible for
determination of the substrate selectivity of MAO A and B (Tsugeno, Y. Hirashiki, I., Ogata, F., and Ito, A. (1995) J. Biochem. (Tokyo) 118, 974-980). To determine the essential amino acids in this region that participate in substrate recognition, a series of mutant enzymes in which amino acid residues that are conserved among various species but are different between the
two forms of the enzyme were replaced with the corresponding amino
acids of the counterpart and were engineered from the cDNAs of rat
liver MAO A and B, and affinities for several substrates were examined.
A single mutation in which Phe-208 in MAO A was substituted by the
corresponding residue of Ile in MAO B was sufficient to convert the
A-type substrate selectivity, and the reverse was exactly the case. Phe
at this position was replaceable with Tyr for the A-type specificity
and Ile was replaceable with Val and Ala for the B-type. Thus, aromatic
and aliphatic residues seem to contribute to render substrate
selectivity of MAO A and MAO B, respectively.
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