Mapování primární struktury methylaminoxidasy z Aspergillus niger obsahující topachinon a měď

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F05%3A00002191" target="_blank" >RIV/61989592:15310/05:00002191 - 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

Mapping the primary structure of copper/topaquinone-containing methylamine oxidase from Aspergillus niger

Popis výsledku v původním jazyce

The amino acid sequence of methylamine oxidase (MeAO) from the fungus Aspergillus niger was analyzed using mass spectrometry (MS). First, MeAO was characterized by an accurate molecular mass of 72.4 kDa of the monomer measured using MALDI-TOF-MS and by apI value of 5.8 determined by isoelectric focusing. MALDI-TOF-MS revealed a clear peptide mass fingerprint after tryptic digestion, which did not provide any relevant hit when searched against a nonredundant protein database and was different from thatof A. niger amine oxidase AO-I. Tandem mass spectrometry with electrospray ionization coupled to liquid chromatography allowed unambiguous reading of six peptide sequences (11-19 amino acids) and seven sequence tags (4-15 amino acids), which were used for MS BLAST homology searching. MeAO was found to be largely homologous to a hypothetical protein AN7641.2 (EMBL/GenBank protein accession code EAA61827) from Aspergillus nidulans FGSC A4 with a theoretical molecular mass of 76 460 Da and

Název v anglickém jazyce

Mapping the primary structure of copper/topaquinone-containing methylamine oxidase from Aspergillus niger

Popis výsledku anglicky

The amino acid sequence of methylamine oxidase (MeAO) from the fungus Aspergillus niger was analyzed using mass spectrometry (MS). First, MeAO was characterized by an accurate molecular mass of 72.4 kDa of the monomer measured using MALDI-TOF-MS and by apI value of 5.8 determined by isoelectric focusing. MALDI-TOF-MS revealed a clear peptide mass fingerprint after tryptic digestion, which did not provide any relevant hit when searched against a nonredundant protein database and was different from thatof A. niger amine oxidase AO-I. Tandem mass spectrometry with electrospray ionization coupled to liquid chromatography allowed unambiguous reading of six peptide sequences (11-19 amino acids) and seven sequence tags (4-15 amino acids), which were used for MS BLAST homology searching. MeAO was found to be largely homologous to a hypothetical protein AN7641.2 (EMBL/GenBank protein accession code EAA61827) from Aspergillus nidulans FGSC A4 with a theoretical molecular mass of 76 460 Da and

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME%20664" target="_blank" >ME 664: Konjugáty proteolytických enzymů ve vysoce výkonné proteomice</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Folia Microbiologica

ISSN

0015-5632

e-ISSN

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Svazek periodika

50

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

8

Strana od-do

401-408

Kód UT WoS článku

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EID výsledku v databázi Scopus

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