"7"^^ . "114" . "94"^^ . . "\u0160ebela, Marek" . . . "15410" . . "Fr\u00E9bort, Ivo" . "8th International Congress on Amino Acids and Proteins" . . "Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger"@en . "Hirota, Shun" . . "Z(MSM 153100013)" . "Tamaki, Hisanori" . "Rome" . . "Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger" . . . . "Heidelberg" . . "Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger"@en . "amine oxidase, Aspergillus niger, gene organization, molecular modelling, primary sequence"@en . . . "Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger" . "Adachi, Osao" . "Pe\u010D, Pavel" . . . "Kumagai, Hidehiko" . "Amine oxidase AO-I from Aspergillus niger AKU 3302 was reported to contain topa quinone as a cofactor, however, the study on p-nitrophe-nylhydrazine derivatized enzyme and purified active site peptides showed the presence of a carboxylate ester linkage of TPQ to a gluta-mate. The catalytic functionality of such a cross-linked cofactor has been shown unlikely by spectroscopic and voltammetric studies on synthe-sized model compounds. We have obtained resonance Raman spectra of native and substrate reduced AO-I showing that the catalytically active cofactor is unmodified TPQ. The primary structure of the enzyme (Gen-Bank U31869) has been reviewed and updated by repeated isolation and sequencing of AO-I cDNA. This allowed rectification of severalerrors that account for previously reported low homology to other amine oxi-dases in the regions around copper binding histididyl residues. The results were confirmed by cloning the ao-1 structural gene (GenBank AF362473). Analysis of the gene 5 -up"@en . "3"^^ . "[3B34519E95FA]" . "RIV/61989592:15410/03:00001356!RIV/2004/MSM/154104/N" . . . . . "608053" . "0"^^ . . "Amine oxidase AO-I from Aspergillus niger AKU 3302 was reported to contain topa quinone as a cofactor, however, the study on p-nitrophe-nylhydrazine derivatized enzyme and purified active site peptides showed the presence of a carboxylate ester linkage of TPQ to a gluta-mate. The catalytic functionality of such a cross-linked cofactor has been shown unlikely by spectroscopic and voltammetric studies on synthe-sized model compounds. We have obtained resonance Raman spectra of native and substrate reduced AO-I showing that the catalytically active cofactor is unmodified TPQ. The primary structure of the enzyme (Gen-Bank U31869) has been reviewed and updated by repeated isolation and sequencing of AO-I cDNA. This allowed rectification of severalerrors that account for previously reported low homology to other amine oxi-dases in the regions around copper binding histididyl residues. The results were confirmed by cloning the ao-1 structural gene (GenBank AF362473). Analysis of the gene 5 -up" . "0939-4451" . "0"^^ . "RIV/61989592:15410/03:00001356" . "Springer-Verlag" .