"60"^^ . "3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins" . . . "Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene" . "15310" . . "RIV/61989592:15310/02:00001496!RIV/2003/MSM/153103/N" . "RIV/61989592:15310/02:00001496" . . "Yamada, Mamoru" . "Amine oxidase AO-I from Aspergillus niger AKU 3302 has been reported to contain topa quinone as the cofactor, however, the study on p-nitrophenylhydrazine derivatised enzyme and purified active site peptides showed the presence of a carboxylate ester linkage of topa to a glutamate [1]. Recently the catalytic functionality of such a crosslinked cofactor has been shown to be unlikely by spectroscopic and voltammetric studies on synthesised model compounds [2]. We have obtained resonance Raman spectra of the AO-I in native state and after reduction with substrate that indeed show that the catalytically active cofactor is unmodified topa quinone. The primary structure of the enzyme [3] (GenBank U31869) has been reviewed by sequencing the AO-I cDNA on a capillary DNA sequencer and shown to contain several frame shifts and errors that account for previously reported lower homology with other amine oxidases in the regions around copper binding histidine residues. The sequence was verified by cloning and sequ"@en . . . "Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene"@en . "Aspergillus niger; active site; amine oxidase; enzyme; gene"@en . "University of Southampton" . "Hirota, Shun" . . . . "6"^^ . "56" . . . "3"^^ . . "Amine oxidase AO-I from Aspergillus niger AKU 3302 has been reported to contain topa quinone as the cofactor, however, the study on p-nitrophenylhydrazine derivatised enzyme and purified active site peptides showed the presence of a carboxylate ester linkage of topa to a glutamate [1]. Recently the catalytic functionality of such a crosslinked cofactor has been shown to be unlikely by spectroscopic and voltammetric studies on synthesised model compounds [2]. We have obtained resonance Raman spectra of the AO-I in native state and after reduction with substrate that indeed show that the catalytically active cofactor is unmodified topa quinone. The primary structure of the enzyme [3] (GenBank U31869) has been reviewed by sequencing the AO-I cDNA on a capillary DNA sequencer and shown to contain several frame shifts and errors that account for previously reported lower homology with other amine oxidases in the regions around copper binding histidine residues. The sequence was verified by cloning and sequ" . "Pe\u010D, Pavel" . . "[2929AD0561F8]" . "Adachi, Osao" . . "Z(MSM 153100010)" . "\u0160ebela, Marek" . "Southampton" . "Fr\u00E9bort, Ivo" . . "Southampton" . "661601" . "0"^^ . . . "0"^^ . . . "Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene" . . "Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene"@en .