ArticleApplied and environmental microbiology2007
Processivity, substrate binding, and mechanism of cellulose hydrolysis by Thermobifida fusca Cel9A.
Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 141 citations in OpenAlex.
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- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
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- Identification of a cell-surface protein involved in glucose assimilation and disruption of the crystalline region of cellulose by Cytophaga hutchinsonii.Journal of industrial microbiology & biotechnology · 2019Article
- Valorization of waste forest biomass toward the production of cello-oligosaccharides with potential prebiotic activity by utilizing customized enzyme cocktails.Biotechnology for biofuels · 2019Article
- Identification and characterization of a hyperthermophilic GH9 cellulase from the Arctic Mid-Ocean Ridge vent field.PloS one · 2019Article
- Novel Insights from Comparative In Silico Analysis of Green Microalgal Cellulases.International journal of molecular sciences · 2018Article
- Advantages of a distant cellulase catalytic base.The Journal of biological chemistry · 2018Article
- Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.Biotechnology for biofuels · 2018Article
- Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase fromBiotechnology for biofuels · 2018Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 2016Article
- Periplasmic Cytophaga hutchinsonii Endoglucanases Are Required for Use of Crystalline Cellulose as the Sole Source of Carbon and Energy.Applied and environmental microbiology · 2016Article
- Production of a functional cell wall-anchored minicellulosome by recombinant Clostridium acetobutylicum ATCC 824.Biotechnology for biofuels · 2016Article
- Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.The Journal of biological chemistry · 2015Article
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- Thermophilic and alkaliphilic Actinobacteria: biology and potential applications.Frontiers in microbiology · 2015Review
- Structure- and context-based analysis of the GxGYxYP family reveals a new putative class of glycoside hydrolase.BMC bioinformatics · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermobifida fusca Cel9A-90 is a processive endoglucanase consisting of a family 9 catalytic domain (CD), a family 3c cellulose binding module (CBM3c), a fibronectin III-like domain, and a family 2 CBM. This enzyme has the highest activity of any individual T. fusca enzyme on crystalline substrates, particularly bacterial cellulose (BC). Mutations were introduced into the CD or the CBM3c of Cel9A-68 using site-directed mutagenesis. The mutant enzymes were expressed in Escherichia coli; purified; and tested for activity on four substrates, ligand binding, and processivity. The results show that H125 and Y206 play an important role in activity by forming a hydrogen bonding network with the catalytic base, D58; another important supporting residue, D55; and Glc(-1) O1. R378, a residue interacting with Glc(+1), plays an important role in processivity. Several enzymes with mutations in the subsites Glc(-2) to Glc(-4) had less than 15% activity on BC and markedly reduced processivity. Mutant enzymes with severalfold-higher activity on carboxymethyl cellulose (CMC) were found in the subsites from Glc(-2) to Glc(-4). The CBM3c mutant enzymes, Y520A, R557A/E559A, and R563A, had decreased activity on BC but had wild-type or improved processivity. Mutation of D513, a conserved residue at the end of the CBM, increased activity on crystalline cellulose. Previous work showed that deletion of the CBM3c abolished crystalline activity and processivity. This study shows that it is residues in the catalytic cleft that control processivity while the CBM3c is important for loose binding of the enzyme to the crystalline cellulose substrate.
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