期刊
ACS SUSTAINABLE CHEMISTRY & ENGINEERING
卷 8, 期 6, 页码 2540-2547出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssuschemeng.9b07073
关键词
alpha-Xylosidase; Crystal structure; Aspergillus niger; Biomass deconstruction; GH31; Specificity
资金
- United States Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-+06CH11357]
- Michigan Economic Development Corp.
- Michigan Technology Tri-Corridor [085P1000817]
- U.S. Department of Energy, DOE Great Lakes Bioenergy Research Center, DOE Office of Science [BER DE-FC02-07ER64494]
- National Institutes of Health [U01 GM098248]
Glycoside hydrolase family 31 (GH31) enzymes show both highly conserved folds and catalytic residues. Yet different members of GH31 show very different substrate specificities, and it is not obvious how these specificities arise from the protein sequences. The fungal alpha-xylosidase, AxlA, was originally isolated from a commercial enzyme mixture secreted by Aspergillus niger and was reported to have potential as a catalytic component in biomass deconstruction in the biofuel industry. We report here the crystal structure of AxlA in complex with its catalytic product, a hydrolyzed xyloglucan oligosaccharide. On the basis of our new structure, we provide the structural basis for AxlA's role in xyloglucan utilization and, more importantly, a new procedure to predict and differentiate C5 vs C6 sugar specific activities based on protein sequences of the functionally diverse GH31 family enzymes.
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