Cloning, sequencing and expression of the cDNA of endoxylanase B from Penicillium purpurogenum.
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).
Díaz
R
R
Laboratorio de Bioquímica, Pontificia Universidad Católica de Chile, Santiago.
Sapag
A
A
Peirano
A
A
Steiner
J
J
Eyzaguirre
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D043364:Endo-1,4-beta Xylanases; D015870:Gene Expression; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology* / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014995:Xylosidases / Q000235:genetics*
D018076:DNA, Complementary; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases