Substrate binding of a GH5 endoglucanase from the ruminal fungusPiromyces rhizinflata
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چکیده
منابع مشابه
Expression and characterization of the Neurospora crassa endoglucanase GH5-1.
Filamentous fungi secrete a wide range of enzymes, including cellulases and hemicellulases, with potential applications in the production of lignocellulosic biofuels. Of the cellulolytic fungi, Hypocrea jecorina (anamorph Trichoderma reesei) is the best characterized in terms of cellulose degradation, but other cellulolytic fungi, such as the model filamentous fungus Neurospora crassa, can serv...
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(a) BlCel5B in the crystallographic and closed configuration; (b) Bacillus halodurans Cel5B (BhCel5B) (PDB id: 4V2X) (c) Piromyces rhizinflata GH5 endoglucanase (PDB id: 3AYR); (d) Clostridium cellulolyticum GH5 endoglucanase (PDB id: 1EDG); (e) Clostridium cellulovorans GH5 endoglucanase (PDB id: 3NDY); (f) Bacteroides ovatus GH5 xyloglucanase (PDB id: 3ZMR); (g) Paenibacillus pabuli GH5 xylog...
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15 صفحه اولCatalytic and substrate-binding domains of endoglucanase 2 from Bacteroides succinogenes.
Endoglucanase 2 (EG2) of the cellulolytic ruminal anaerobe Bacteroides succinogenes is a 118-kilodalton (kDa) enzyme which binds to cellulose and produces cellotetraose as the end product of hydrolysis. The purified enzyme was treated with the protease trypsin in an attempt to isolate peptides which retained the ability to either hydrolyze soluble carboxymethyl cellulose or bind to insoluble ce...
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Northern (RNA) blot analysis of RNA from Clostridium sp. revealed induction of transcription of the celA gene when barley beta-glucan was used as carbon source, while no celA mRNA was detected after growth on cellobiose. Western blots (immunoblots), prepared by using a rabbit antiserum raised against CelA protein purified from Escherichia coli, revealed the extracellular location of CelA in Clo...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2011
ISSN: 1744-3091
DOI: 10.1107/s1744309111032428