@article { ISI:000085378200062,
	title = {Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger beta-glucosidase},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {275},
	number = {7},
	year = {2000},
	month = {FEB 18},
	pages = {4973-4980},
	abstract = {{The beta-glucosidase from Aspergillus niger (CMI. CC 324262) was purified, and an N-terminal sequence and two internal sequences were determined. BglI genomic gene and the cDNA were cloned from a genomic library and by reverse transcriptase-polymerase chain reaction, respectively. The cDNA was successfully expressed in Saccharomyces cerevisiae and Pichia pastoris. Sequence analysis revealed that the gene encodes a 92-kDa enzyme that is a member of glycosidase family 3. H-1-NMR analysis of the reaction catalyzed by this enzyme confirmed that, in common with other family 3 glycosidases, this enzyme hydrolyzes with net retention of anomeric configuration. Accordingly, the enzyme was inactivated by a-deoxy-a-fluoro beta-glucosyl fluoride, with kinetic parameters of k(i) = 4.5 min(-1)},
	issn = {0021-9258},
	doi = {10.1074/jbc.275.7.4973},
	author = {Dan, S and Marton, I and Dekel, M and Bravdo, BA and He, SM and Withers, SG and Shoseyov, O}
}
