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

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Gene organization and molecular modeling of copper amine oxidase from Aspergillus niger
Original language 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 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
Czech name
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Czech description
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Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection
8th International Congress on Amino Acids and Proteins
ISBN
0939-4451
ISSN
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e-ISSN
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Number of pages
94
Pages from-to
114
Publisher name
Springer
Place of publication
Heidelberg
Event location
Rome
Event date
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Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
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