What is it about?
Discovery and characterisation of a GH27 enzyme that specifically cleaves B-l-arabinopyranose residues from arabinogalactan, and is secreted by the bacterium Chitinophaga pinensis for this purpose. We demonstrate by site directed mutagenesis that an active site isoleucine is responsible for the remarkably high level of specificity of this enzyme, which has no activity at all against the similar A-d-galactopyranose structure.
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Why is it important?
The identification of this specificity-determining isoleucine allowed us to construct a phylogenetic tree that likely has predictive value for family GH27.
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This page is a summary of: Growth of Chitinophaga pinensis on Plant Cell Wall Glycans and Characterisation of a Glycoside Hydrolase Family 27 β-l-Arabinopyranosidase Implicated in Arabinogalactan Utilisation, PLoS ONE, October 2015, PLOS,
DOI: 10.1371/journal.pone.0139932.
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