About: Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene

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About: Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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 (en)
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 (en)
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 (en)
skos:notation	RIV/61989592:15310/02:00001496!RIV/2003/MSM/153103/N
http://linked.open.../vavai/riv/strany	56
http://linked.open...avai/riv/aktivita	Z
http://linked.open...avai/riv/aktivity	Z(MSM 153100010)
http://linked.open...vai/riv/dodaniDat	2003
http://linked.open...aciTvurceVysledku	Peč, Pavel Šebela, Marek Frébort, Ivo
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	661601
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/02:00001496
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Aspergillus niger; active site; amine oxidase; enzyme; gene (en)
http://linked.open.../riv/klicoveSlovo	Aspergillus niger amine oxidase gene enzyme active site
http://linked.open...ontrolniKodProRIV	[2929AD0561F8]
http://linked.open...v/mistoKonaniAkce	Southampton
http://linked.open...i/riv/mistoVydani	Southampton
http://linked.open...i/riv/nazevZdroje	3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...UplatneniVysledku	2002
http://linked.open...iv/tvurceVysledku	Šebela, Marek Frébort, Ivo Peč, Pavel Adachi, Osao Yamada, Mamoru Hirota, Shun
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20153100010
number of pages	60 (xsd:int)
http://purl.org/ne...btex#hasPublisher	University of Southampton
http://localhost/t...ganizacniJednotka	15310

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