Mapping the primary structure of copper/topaquinone-containing methylamine oxidase from Aspergillus niger
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
16475499
DOI
10.1007/bf02931421
Knihovny.cz E-zdroje
- MeSH
- Aspergillus niger enzymologie genetika MeSH
- chromatografie kapalinová MeSH
- dihydroxyfenylalanin analogy a deriváty analýza MeSH
- hmotnostní spektrometrie s elektrosprejovou ionizací MeSH
- isoelektrická fokusace MeSH
- izoelektrický bod MeSH
- měď analýza MeSH
- molekulární sekvence - údaje MeSH
- molekulová hmotnost MeSH
- oxidoreduktasy působící na CH-NH vazby chemie genetika MeSH
- peptidové mapování MeSH
- sekvence aminokyselin MeSH
- sekvenční analýza proteinů * MeSH
- sekvenční homologie aminokyselin MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- trypsin metabolismus MeSH
- výpočetní biologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 6-hydroxydopa quinone MeSH Prohlížeč
- dihydroxyfenylalanin MeSH
- měď MeSH
- methylamine dehydrogenase MeSH Prohlížeč
- oxidoreduktasy působící na CH-NH vazby MeSH
- trypsin MeSH
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 molar mass of 72.4 kDa of the monomer measured using MALDI-TOF-MS and by a pI 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 that of 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 molar mass of 76.46 kDa and pI 6.14, which belongs to the superfamily of copper amine oxidases. The protein AN7641.2 is only little homologous to the amine oxidase AO-I (32% identity, 49 % similarity).
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