刊名:International Journal of Biological Macromolecules
出版年:2013
出版时间:September, 2013
年:2013
卷:60
期:Complete
页码:109-115
全文大小:3751 K
文摘
The crystal structure of the industrially important Aspergillus oryzae ¦Â-galactosidase has been determined at 2.60 ? resolution. The Ao-¦Â-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (¦Á/¦Â)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-¦Â-gal. Comparison of structure with other ¦Â-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-¦Â-gal is also discussed.