Structure of the cel-3 gene from Fibrobacter succinogenes S85 and characteristics of the encoded gene product, endoglucanase 3
نویسندگان
چکیده
منابع مشابه
Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85.
The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain displayed an activity profile typical of an endoglucanase, with high catalytic activity on carboxymethyl...
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Cells of the anaerobic ruminal bacterium Fibrobacter succinogenes subsp. succinogenes S85 (formerly Bacteroides succinogenes) exhibit arylesterase activity. When cells were grown on cellulose, it was found that 69% of the total esterase activity was extracellular while 65% was nonsedimentable upon centrifugation of the culture supernatant at 100,000 x g. Disruption of the cells by various diffe...
متن کاملA novel family 9 endoglucanase gene (celD), whose product cleaves substrates mainly to glucose, and its adjacent upstream homolog (celE) from Fibrobacter succinogenes S85.
Two adjacent, highly homologous endoglucanase genes, celD and celE from Fibrobacter succinogenes S85, which were separated by an AT-rich 223-nucleotide intergenic region were characterized. The celD gene codes for endoglucanase D (EGD), a protein of 668 residues with a molecular mass of 71.7 kDa, while the celE gene encodes endoglucanase E, a protein of 467 amino acids with a molecular mass of ...
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15 صفحه اولGene sequence analysis and properties of EGC, a family E (9) endoglucanase from Fibrobacter succinogenes BL2.
The endoglucanase gene (endC) of Fibrobacter succinogenes BL2 encodes a protein of 620 amino acids (EGC) that shows similarity with family E1 cellulases, and particularly with EGB from F. succinogenes S85. Alignment of the amino acid sequence of family E1 cellulases revealed that EGC is composed of a N-terminal domain and a large catalytic domain of 453 residues containing an extension of 60 re...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1989
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.171.10.5587-5595.1989