Functional expression of amine oxidase from Aspergillus niger (AO-I) in Saccharomyces cerevisiae
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Amines metabolism MeSH
- Aspergillus niger enzymology genetics MeSH
- Chromatography, DEAE-Cellulose MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Amine Oxidase (Copper-Containing) chemistry genetics metabolism MeSH
- Mass Spectrometry MeSH
- Kinetics MeSH
- Cloning, Molecular MeSH
- Molecular Sequence Data MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amines MeSH
- Fungal Proteins MeSH
- hexylamine MeSH Browser
- Amine Oxidase (Copper-Containing) MeSH
- Recombinant Proteins MeSH
The aim of this work was to prepare recombinant amine oxidase from Aspergillus niger after overexpressing in yeast. The yeast expression vector pDR197 that includes a constitutive PMA1 promoter was used for the expression in Saccharomyces cerevisiae. Recombinant amine oxidase was extracted from the growth medium of the yeast, purified to homogeneity and identified by activity assay and MALDI-TOF peptide mass fingerprinting. Similarity search in the newly published A. niger genome identified six genes coding for copper amine oxidase, two of them corresponding to the previously described enzymes AO-I a methylamine oxidase and three other genes coding for FAD amine oxidases. Thus, A. niger possesses an enormous metabolic gear to grow on amine compounds and thus support its saprophytic lifestyle.
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