Mapping the primary structure of copper/topaquinone-containing methylamine oxidase from Aspergillus niger
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16475499
DOI
10.1007/bf02931421
Knihovny.cz E-resources
- MeSH
- Aspergillus niger enzymology genetics MeSH
- Chromatography, Liquid MeSH
- Dihydroxyphenylalanine analogs & derivatives analysis MeSH
- Spectrometry, Mass, Electrospray Ionization MeSH
- Isoelectric Focusing MeSH
- Isoelectric Point MeSH
- Copper analysis MeSH
- Molecular Sequence Data MeSH
- Molecular Weight MeSH
- Oxidoreductases Acting on CH-NH Group Donors chemistry genetics MeSH
- Peptide Mapping MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, Protein * MeSH
- Sequence Homology, Amino Acid MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Trypsin metabolism MeSH
- Computational Biology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 6-hydroxydopa quinone MeSH Browser
- Dihydroxyphenylalanine MeSH
- Copper MeSH
- methylamine dehydrogenase MeSH Browser
- Oxidoreductases Acting on CH-NH Group Donors 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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