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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F02%3A00001496%21RIV%2F2003%2FMSM%2F153103%2FN
rdf:type
n18:Vysledek skos:Concept
dcterms:description
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 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
dcterms:title
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
skos:prefLabel
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
skos:notation
RIV/61989592:15310/02:00001496!RIV/2003/MSM/153103/N
n4:strany
56
n4:aktivita
n20:Z
n4:aktivity
Z(MSM 153100010)
n4:dodaniDat
n9:2003
n4:domaciTvurceVysledku
n6:9708790 n6:4536274 n6:5433851
n4:druhVysledku
n12:D
n4:duvernostUdaju
n19:S
n4:entitaPredkladatele
n17:predkladatel
n4:idSjednocenehoVysledku
661601
n4:idVysledku
RIV/61989592:15310/02:00001496
n4:jazykVysledku
n11:eng
n4:klicovaSlova
Aspergillus niger; active site; amine oxidase; enzyme; gene
n4:klicoveSlovo
n5:Aspergillus%20niger n5:amine%20oxidase n5:active%20site n5:enzyme n5:gene
n4:kontrolniKodProRIV
[2929AD0561F8]
n4:mistoKonaniAkce
Southampton
n4:mistoVydani
Southampton
n4:nazevZdroje
3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins
n4:obor
n15:CE
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
6
n4:pocetUcastnikuAkce
0
n4:pocetZahranicnichUcastnikuAkce
0
n4:rokUplatneniVysledku
n9:2002
n4:tvurceVysledku
Yamada, Mamoru Hirota, Shun Peč, Pavel Adachi, Osao Šebela, Marek Frébort, Ivo
n4:typAkce
n16:WRD
n4:zamer
n14:MSM%20153100010
s:numberOfPages
60
n13:hasPublisher
University of Southampton
n8:organizacniJednotka
15310