Molecular characteristics of a single and novel form of carp (Cyprinus carpio) monoamine oxidase.
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.
Sugimoto
Haruyo
H
Department of Pharmacology, School of Medicine, Showa University, 1-5-8 Hatanodai, Shinagawa-Ku, Tokyo 142-8555, Japan. countryroad_go@yahoo.co.jp
Taguchi
Yu-Dai
YD
Shibata
Kiyotaka
K
Kinemuchi
Hiroyasu
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002347:Carps / Q000235:genetics; D002462:Cell Membrane / Q000378:metabolism; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D018076:DNA, Complementary; D008996:Monoamine Oxidase Inhibitors; D005182:Flavin-Adenine Dinucleotide; D008995:Monoamine Oxidase