Functional Analysis of Genes Encoding Putative Oxidoreductases in Aspergillus oryzae, Which Are Similar to Fungal Fructosyl-Amino Acid Oxidase
Autor: | Tetsuya Karino, Nobuyuki Yoshida, Yoji Hata, Shin-ichi Akazawa, Hiroshi Takagi, Hiroki Ishida, Tohoru Katsuragi, Yoshiki Tani |
---|---|
Rok vydání: | 2007 |
Předmět: |
DNA
Complementary Sarcosine Proline Sequence analysis Aspergillus oryzae Genes Fungal Molecular Sequence Data Bioengineering Biology Applied Microbiology and Biotechnology Isozyme Substrate Specificity Fungal Proteins chemistry.chemical_compound Sequence Analysis Protein Escherichia coli Amino Acid Sequence Cloning Molecular Peptide sequence Gene Phylogeny chemistry.chemical_classification Oxidase test biology.organism_classification Enzyme Biochemistry chemistry Pipecolic Acids Amino Acid Oxidoreductases Biotechnology |
Zdroj: | Journal of Bioscience and Bioengineering. 104:424-427 |
ISSN: | 1389-1723 |
Popis: | We found 11 genes (FAO1-11) encoding putative oxidoreductases in the Aspergillus oryzae genome, which are similar to fungal fructosyl-amino acid oxidases. The cDNAs corresponding to the genes were cloned and expressed in Escherichia coli. rFao2 had fructosyl-amino acid oxidase activity, whereas rFao1 did not show any enzyme activity, even though the deduced amino acid sequence of Fao1 is identical to that of one of the fructosyl-amino acid oxidase isozymes from Aspergillus oryzae. rFao7 and rFao8 showed oxidase activity toward sarcosine, L-pipecolate, and L-proline. rFao10 was active toward only sarcosine, of the substrates tested. The functions of the other proteins were also predicted from a phylogenetic analysis. |
Databáze: | OpenAIRE |
Externí odkaz: |