Cloning of Clostridium cellulovorans endo-1,4-beta...[Biochem Biophys Res Commun. 1990]

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1: Biochem Biophys Res Commun. 1990 Jun 15;169(2):667-72. Links

Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes.

Shoseyov O, Hamamoto T, Foong F, Doi RH.

Department of Biochemistry and Biophysics, University of California, Davis 95616.

A Clostridium cellulovorans lambda gt11 gene bank was screened for endo-1,4-beta-glucanase [EC 3.2.1.4, EGase, Carboxy Methyl Cellulase (CMCase)] genes using a chromogenic substrate. Three genes (engA, engB, and engC) were isolated. The engB expressed the most active CMCase. The engA encoded a bifunctional enzyme that displayed endo-1,4-beta-glucanase and beta-glucosidase activities. The three recombinant glucanases, when expressed in Escherichia coli, were partially degraded into multiform active enzymes as evidenced by their SDS-PAGE-CMC zymograms. None of the clones could degrade crystalline cellulose, thus supporting the hypothesis that the integrity of the C. cellulovorans cellulase complex was essential for its 'true cellulase' activity.

PMID: 2113383 [PubMed - indexed for MEDLINE]

Heterologous expression of endo-beta-1,4-D-glucanase from Clostridium cellulovorans in Clostridium acetobutylicum ATCC 824 following transformation of the engB gene.
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[Appl Environ Microbiol. 1994]
Characterization and comparison of Clostridium cellulovorans endoglucanases-xylanases EngB and EngD hyperexpressed in Escherichia coli.
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Cloning of an endo-(1-->4)-beta-glucanase gene, celA, from the rumen bacterium Clostridium sp. ('C. longisporum') and characterization of its product, CelA, in Escherichia coli.
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[J Gen Microbiol. 1993]
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[Curr Top Dev Biol. 1999]
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Chem Rec. 2001; 1(1):24-32.

[Chem Rec. 2001]
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