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  • Title: Molecular characteristics of a single and novel form of carp (Cyprinus carpio) monoamine oxidase.
    Author: Sugimoto H, Taguchi YD, Shibata K, Kinemuchi H.
    Journal: Comp Biochem Physiol B Biochem Mol Biol; 2010 Mar; 155(3):266-71. PubMed ID: 19932189.
    Abstract:
    Two mammalian monoamine oxidases (MAO), MAO-A and MAO-B, are similar in primary structures but have unique substrate/inhibitor selectivities. Carp (Cyprinus carpio) contains a MAO enzyme (C-MAO) with properties different from MAO-A and MAO-B. To determine the molecular characteristics of C-MAO and its phylogenetic relationship with other fish and mammalian MAOs, the primary structure of C-MAO was estimated. The putative C-MAO cDNA encodes 526 amino acids with 59.001 Da, and the deduced amino acid sequence showed as much as 68.9% homology with some mammalian MAO-A proteins, 69.8% homology with some mammalian MAO-B proteins, and as much as 92.4% homology with some fish MAOs. Comparison of two regions in the polypeptide sequence of C-MAO determining possible substrate/inhibitor preferences of MAO-A and MAO-B showed both 79.5% homologies.
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