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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001496" target="_blank" >RIV/61989592:15310/02:00001496 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Reassessment of the active site of the amine oxidase AO-I from Aspergillus niger AKU 3302 and a structure of the coding gene
Original language 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
Czech name
—
Czech description
—

Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection
3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins
ISBN
—
ISSN
—
e-ISSN
—
Number of pages
60
Pages from-to
56
Publisher name
University of Southampton
Place of publication
Southampton
Event location
Southampton
Event date
—
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
—

Similar results(10)