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Statements

Subject Item
n2:RIV%2F61989592%3A15410%2F03%3A00001356%21RIV%2F2004%2FMSM%2F154104%2FN
rdf:type
n12:Vysledek skos:Concept
dcterms: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
dcterms: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
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
skos:notation
RIV/61989592:15410/03:00001356!RIV/2004/MSM/154104/N
n3:strany
114
n3:aktivita
n11:Z
n3:aktivity
Z(MSM 153100013)
n3:dodaniDat
n14:2004
n3:domaciTvurceVysledku
n10:5433851 n10:9708790 n10:4536274
n3:druhVysledku
n16:D
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n19:predkladatel
n3:idSjednocenehoVysledku
608053
n3:idVysledku
RIV/61989592:15410/03:00001356
n3:jazykVysledku
n15:eng
n3:klicovaSlova
amine oxidase, Aspergillus niger, gene organization, molecular modelling, primary sequence
n3:klicoveSlovo
n5:gene%20organization n5:molecular%20modelling n5:primary%20sequence n5:Aspergillus%20niger n5:amine%20oxidase
n3:kontrolniKodProRIV
[3B34519E95FA]
n3:mistoKonaniAkce
Rome
n3:mistoVydani
Heidelberg
n3:nazevZdroje
8th International Congress on Amino Acids and Proteins
n3:obor
n18:CE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
7
n3:pocetUcastnikuAkce
0
n3:pocetZahranicnichUcastnikuAkce
0
n3:rokUplatneniVysledku
n14:2003
n3:tvurceVysledku
Šebela, Marek Frébort, Ivo Hirota, Shun Tamaki, Hisanori Adachi, Osao Peč, Pavel Kumagai, Hidehiko
n3:typAkce
n8:WRD
n3:zamer
n17:MSM%20153100013
s:issn
0939-4451
s:numberOfPages
94
n20:hasPublisher
Springer-Verlag
n7:organizacniJednotka
15410