2WSP

Thermotoga maritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3

Summary for 2WSP

• Entry DOI: 10.2210/pdb2wsp/pdb
• Related: 1HL8 1HL9 1ODU
• Descriptor: ALPHA-L-FUCOSIDASE, PUTATIVE, alpha-L-fucopyranose-(1-2)-beta-L-fucosyl-azide (3 entities in total)
• Functional Keywords: hydrolase, glycoside hydrolase, carbohydrate synthesis, thermophilic enzyme
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 2
• Total formula weight: 105100.66

Authors

Sulzenbacher, G.,Lipski, A.,Cobucci-Ponzano, B.,Conte, F.,Bedini, E.,Corsaro, M.M.,Parrilli, M.,Dal Piaz, F.,Lepore, L.,Rossi, M.,Moracci, M. (deposition date: 2009-09-08, release date: 2010-01-19, Last modification date: 2024-10-09)

Primary citation

Cobucci-Ponzano, B.,Conte, F.,Bedini, E.,Corsaro, M.M.,Parrilli, M.,Sulzenbacher, G.,Lipski, A.,Dal Piaz, F.,Lepore, L.,Rossi, M.,Moracci, M.
Beta-Glycosyl Azides as Substrates for Alpha-Glycosynthases: Preparation of Novel Efficient Alpha-L-Fucosynthases
Chem.Biol., 16:1097-, 2009

PubMed Abstract: Fucose-containing oligosaccharides play a central role in physio-pathological events, and fucosylated oligosaccharides have interesting potential applications in biomedicine. No methods for the large-scale production of oligosaccharides are currently available, but the chemo-enzymatic approach is very promising. Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, have been demonstrated to be an interesting alternative. However, examples of glycosynthases available so far are restricted to a limited number of glycosidases families and to only one retaining alpha-glycosynthase. We show here that new mutants of two alpha-L-fucosidases are efficient alpha-L-fucosynthases. The approach shown utilized beta-L-fucopyranosyl azide as donor substrate leading to transglycosylation yields up to 91%. This is the first method exploiting a beta-glycosyl azide donor for alpha-glycosynthases; its applicability to the glycosynthetic methodology in a wider perspective is presented.

PubMed: 19875083
DOI: 10.1016/J.CHEMBIOL.2009.09.013

Experimental method

X-RAY DIFFRACTION (2.65 Å)