Abstract
Complementary DNA encoding pyranose oxidase (PROD) was cloned and sequenced for the first time from Coriolus versicolor. The nucleotide sequence revealed an open reading frame encoding a polypeptide composed of 623 amino acid residues. Compared with the experimentally determined N-terminal sequence of the PROD from C. versicolor. 38 amino acids from the N-terminus of the protein appeared to be eliminated during protein maturation. The cDNA was successfully expressed under the control of lacUV5 promoter in Escherichia coli at 25 degrees C, which will be beneficial in industrial production.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Basidiomycota / enzymology*
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Basidiomycota / genetics
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Carbohydrate Dehydrogenases / biosynthesis*
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Carbohydrate Dehydrogenases / genetics*
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Carbohydrate Dehydrogenases / metabolism
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Cloning, Molecular
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DNA, Complementary / genetics
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Industrial Microbiology / methods
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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DNA, Complementary
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Peptide Fragments
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Recombinant Proteins
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Carbohydrate Dehydrogenases
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pyranose oxidase