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Appl Environ Microbiol. 2011 Sep;77(17):6274-6. doi: 10.1128/AEM.05532-11. Epub 2011 Jul 15.

Determination of the catalytic base in family 48 glycosyl hydrolases.

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  • 1Department of Molecular Biology and Genetics, Cornell University, 458 Biotechnology Building, Ithaca, NY 14853, USA.

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.

PMID:
21764975
[PubMed - indexed for MEDLINE]
PMCID:
PMC3165399
Free PMC Article

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