Structural highlights
Publication Abstract from PubMed
Structure-guided active-site redesign of a family GT-80 beta-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from alpha-2,3 in the wild type to alpha-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.
Complete switch from alpha-2,3- to alpha-2,6-regioselectivity in Pasteurella dagmatis beta-D-galactoside sialyltransferase by active-site redesign.,Schmolzer K, Czabany T, Luley-Goedl C, Pavkov-Keller T, Ribitsch D, Schwab H, Gruber K, Weber H, Nidetzky B Chem Commun (Camb). 2015 Feb 21;51(15):3083-6. doi: 10.1039/c4cc09772f. PMID:25619424[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schmolzer K, Czabany T, Luley-Goedl C, Pavkov-Keller T, Ribitsch D, Schwab H, Gruber K, Weber H, Nidetzky B. Complete switch from alpha-2,3- to alpha-2,6-regioselectivity in Pasteurella dagmatis beta-D-galactoside sialyltransferase by active-site redesign. Chem Commun (Camb). 2015 Feb 21;51(15):3083-6. doi: 10.1039/c4cc09772f. PMID:25619424 doi:http://dx.doi.org/10.1039/c4cc09772f
