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  • 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
  • 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)
Title
  • Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger
  • Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger (en)
skos:prefLabel
  • Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger
  • Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger (en)
skos:notation
  • RIV/61989592:15410/03:00001356!RIV/2004/MSM/154104/N
http://linked.open.../vavai/riv/strany
  • 114
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  • Z(MSM 153100013)
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  • 608053
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  • RIV/61989592:15410/03:00001356
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  • amine oxidase, Aspergillus niger, gene organization, molecular modelling, primary sequence (en)
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  • [3B34519E95FA]
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  • Rome
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  • Heidelberg
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  • 8th International Congress on Amino Acids and Proteins
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  • Šebela, Marek
  • Frébort, Ivo
  • Peč, Pavel
  • Adachi, Osao
  • Hirota, Shun
  • Kumagai, Hidehiko
  • Tamaki, Hisanori
http://linked.open...vavai/riv/typAkce
http://linked.open...n/vavai/riv/zamer
issn
  • 0939-4451
number of pages
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  • Springer-Verlag
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  • 15410
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