Cloning, sequencing and expression of the cDNA of endoxylanase B from Penicillium purpurogenum
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Date
1997
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Abstract
The cDNA, for xylanase B from Penicillium purpurogenum was cloned and sequenced. This DNA encodes a protein of 208 amino acids which is expected to yield a protein of 183 residues upon processing of the N terminus. The sequence of the predicted protein is very similar to that of 40 other xylanase domains which belong to family G of cellulases/xylanases (73-21% identity).
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Keywords
endoxylanase, P-purpurogenum, nucleotide sequence, glycosyl hydrolase, PCR, sequence alignment, homology comparison, codon usage