ArticleApplied and environmental microbiology2011
Determination of the catalytic base in family 48 glycosyl hydrolases.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- In Silico Study of Potential Binding Sites of the Family GH126 Enzyme CPF_2247 fromMolecules (Basel, Switzerland) · 2026Article
- Determination of the native features of the exoglucanase Cel48S fromBiotechnology for biofuels · 2018Article
- The GH130 Family of Mannoside Phosphorylases Contains Glycoside Hydrolases That Target β-1,2-Mannosidic Linkages in Candida Mannan.The Journal of biological chemistry · 2015Article
- Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.Acta crystallographica. Section F, Structural biology communications · 2015Article
- C/N ratio drives soil actinobacterial cellobiohydrolase gene diversity.Applied and environmental microbiology · 2015Article
- Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F.Enzyme research · 2014Article
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Authors and funding
2 authors.
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Abstract
The catalytic base in family 48 glycosyl hydrolases has not been previously established experimentally. Based on structural and modeling data published to date, we used site-directed mutagenesis and azide rescue activity assays to show definitively that the catalytic base in Thermobifida fusca Cel48A is aspartic acid 225. Of the tested mutants, only Cel48A with the D225E mutation retained partial activity on soluble and insoluble substrates. In azide rescue experiments, only the D225G mutation, in the smallest residue tested, showed an increase in activity with added azide.
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