Purification and characterization of an endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene
Article Abstract:
The celA gene of Streptomyces lividans, which encodes an endoglucanase, was cloned and characterized. Sequence analysisof the gene revealed an open reading frame coding for a protein of 46,027 Da. The deduced N-terminal amino acid sequence showed significant homologies to cellulose binding domains, suggesting the same functional role for the S. lividans endoglucanase. The catalytic domain was localized to the central part of the protein. Sequence comparisons with other endoglucanases revealed two conserved amino acid residues, His-222 and Glu-259, which are probably involvedin the active site.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans
Article Abstract:
The changes in the signal peptide, xylanase A, affects the level of its production in Streptomyces lividans. The removal of the signal peptide or a change in its cleavage site stops secretion of the enzyme. Substitution of the signal peptide with those of xylanase B, cellulase A, mannanase or acetylxylan esterase has no effect on enzyme production. Substitution with the signal peptides of cellulase B, xylanase C, and LamB decreases enzyme formation. The difference in production is due to the nature of the signal sequences as all the clones have the same transcription levels.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Increase in xylanase production by Streptomyces lividans through simultaneous use of the sec- and tat- dependent protein export systems
Article Abstract:
Xylanase B1 (XlnB1) from Streptomyces lividans is a protein consisting of two discrete structural and functional units, a N-terminal catalytic domain and a C-terminal substrate-binding domain. In the culture medium, two forms of xylanase B are present, namely XInB1 and XInB2.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
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