Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15410%2F03%3A00001356" target="_blank" >RIV/61989592:15410/03:00001356 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger

Popis výsledku v původním jazyce

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 reducedAO-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 -u

Název v anglickém jazyce

Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger

Popis výsledku anglicky

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 reducedAO-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 -u

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

8th International Congress on Amino Acids and Proteins

ISBN

0939-4451

ISSN

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e-ISSN

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Počet stran výsledku

94

Strana od-do

114

Název nakladatele

Springer

Místo vydání

Heidelberg

Místo konání akce

Rome

Datum konání akce

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Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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