Works (1)

Updated: July 5th, 2023 15:39

2016 journal article

Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species

JOURNAL OF BIOLOGICAL CHEMISTRY, 291(13), 6732–6747.

By: J. Conway n, W. Pierce n, J. Le n, G. Harper n, J. Wright n, A. Tucker n, J. Zurawski n, L. Lee n, S. Blumer-Schuette n, R. Kelly n

author keywords: biofuel; cell surface; cell surface enzyme; enzyme; glycoside hydrolase; plant cell wall; Caldicellulosiruptor; S-layer; lignocellulose
MeSH headings : Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Cloning, Molecular; Clostridiales / chemistry; Clostridiales / classification; Clostridiales / enzymology; Escherichia coli / genetics; Escherichia coli / metabolism; Gene Expression; Genome, Bacterial; Glucans / metabolism; Glycoside Hydrolases / chemistry; Glycoside Hydrolases / genetics; Glycoside Hydrolases / metabolism; Kinetics; Mutation; Phylogeny; Polysaccharides / metabolism; Protein Binding; Protein Engineering; Protein Structure, Tertiary; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Substrate Specificity; Wood / metabolism; Xylans / metabolism
TL;DR: The results here provide new insights into the architecture and role of SLHdomain GHs and demonstrate that hemicellulose degradation can be enhanced through non-native SLH domain GHs engineered into the genomes of Caldicelluosiruptor species. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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