Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8333263 | International Journal of Biological Macromolecules | 2013 | 7 Pages |
Abstract
The crystal structure of the industrially important Aspergillus oryzae β-galactosidase has been determined at 2.60 Ã
resolution. The Ao-β-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (α/β)8-barrel domain. An electron density map revealed extensive N-glycosylation between the domain interfaces suggesting that the oligosaccharide-chains would have a stabilizing role for the structure of Ao-β-gal. Comparison of structure with other β-galactosidase structures of glycoside hydrolase family 35 revealed a number of hydrophobic residues, which may contribute favorably to the stabilization of the structure. The role of a high number of acidic residues in Ao-β-gal is also discussed.
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Authors
Mirko M. Maksimainen, Anja Lampio, Mirka Mertanen, Ossi Turunen, Juha Rouvinen,