Amine oxidases from Aspergillus niger : identification of a novel flavin-dependent enzyme

摘要: Upon induction with various amine sources, two different oxidases are expressed in the filamentous fungus Aspergillus niger. The enzymes which can be separated by anion exchange chromatography exhibit a similar substrate specificity pattern. From cofactor and inhibitor analysis it was found that one oxidase is identical to earlier reported copper-containing (Yamada, H., Adachi, O. Ogata, K. (1965) Agric. Biol. Chem. 29, 912-917) 6-hydroxydopa (TOPA) quinone as active site cofactor. second form hitherto unknown flavoprotein of 55 kDa, shows many characteristic properties mammalian monoamine (MAO). susceptibility, suggested from A. niger (MAO-N) prototype enzymes, MAO-A MAO-B. A partial cDNA clone encodes an amino-terminal peptide 53 amino acid residues identified lambda gt11 immunoscreening. consensus sequence putative flavin adenine dinucleotide (FAD) binding within this sequence.