Structural highlights
Function
[BGALA_ASPOR] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans (By similarity).
Publication Abstract from PubMed
The crystal structure of the industrially important Aspergillus oryzae beta-galactosidase has been determined at 2.60A resolution. The Ao-beta-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (alpha/beta)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-beta-gal. Comparison of structure with other beta-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-beta-gal is also discussed.
The crystal structure of acidic beta-galactosidase from Aspergillus oryzae.,Maksimainen MM, Lampio A, Mertanen M, Turunen O, Rouvinen J Int J Biol Macromol. 2013 Sep;60:109-15. doi: 10.1016/j.ijbiomac.2013.05.003., Epub 2013 May 17. PMID:23688418[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maksimainen MM, Lampio A, Mertanen M, Turunen O, Rouvinen J. The crystal structure of acidic beta-galactosidase from Aspergillus oryzae. Int J Biol Macromol. 2013 Sep;60:109-15. doi: 10.1016/j.ijbiomac.2013.05.003., Epub 2013 May 17. PMID:23688418 doi:10.1016/j.ijbiomac.2013.05.003
