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rdf:type
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Description
| - 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)
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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)
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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)
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skos:notation
| - RIV/61989592:15410/03:00001356!RIV/2004/MSM/154104/N
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http://linked.open.../vavai/riv/strany
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15410/03:00001356
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - amine oxidase, Aspergillus niger, gene organization, molecular modelling, primary sequence (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...ontrolniKodProRIV
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http://linked.open...v/mistoKonaniAkce
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http://linked.open...i/riv/mistoVydani
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http://linked.open...i/riv/nazevZdroje
| - 8th International Congress on Amino Acids and Proteins
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...ocetUcastnikuAkce
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http://linked.open...nichUcastnikuAkce
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http://linked.open...UplatneniVysledku
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http://linked.open...iv/tvurceVysledku
| - Šebela, Marek
- Frébort, Ivo
- Peč, Pavel
- Adachi, Osao
- Hirota, Shun
- Kumagai, Hidehiko
- Tamaki, Hisanori
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http://linked.open...vavai/riv/typAkce
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://purl.org/ne...btex#hasPublisher
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http://localhost/t...ganizacniJednotka
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