Article Figures & Data
Figures
- Fig 1
Stability of the α-l-fucosidases AlfB (●) and AlfC (○). The enzymes (10 μg/ml) were incubated in 100 mM sodium phosphate buffer at pH 7.0 and 42�C, and the residual activities were determined at different time intervals with 2 mM p-nitrophenyl α-l-fucopyranoside as the substrate. The initial activity was defined as 100%. The data presented are mean values from three replicate experiments. The errors bars represent the standard deviations.
- Fig 2
(A and B) Partial 1D 1H NMR spectra (600 MHz, 313 K) covering the anomeric region of commercial fucosyl-α-1,3-N-acetylglucosamine (Fuc-α-1,3-GlcNAc) (A) and the transfucosylation reaction with AlfB (B). (C) 1H, 13C-HSQC of Fuc-α-1,3-GlcNAc (red) and the reaction mixture (black).
- Fig 3
(A and B) Partial 1D 1H NMR spectra (600 MHz, 313 K) covering the anomeric region of commercial fucosyl-α-1,6-N-acetylglucosamine (Fuc-α-1,6-GlcNAc) (A) and the transfucosylation reaction with AlfC (B). (C) 1H, 13C-HSQC of Fuc-α-1,6-GlcNAc (red) and the reaction mixture (black).
- Fig 4
Time course of the substrate consumption and the product formation by transfucosylation catalyzed by α-l-fucosidases AlfB (A) and AlfC (B). ●, p-nitrophenyl-α-l-fucopyranoside; ◆, p-nitrophenol; ▼, l-fucose; ■, fucosyl-α-1,3-N-acetylglucosamine; □, fucosyl-α-1,6-N-acetylglucosamine. Data from a representative experiment are shown.
Tables
- Table 1
Transglycosylation and hydrolysis activities of AlfB and AlfC
Enzyme Transglycosylation (μmol/min/mg protein) Hydrolysis (μmol/min/mg protein) Vtrans/Vhyda AlfB 0.95 1.50 0.63 AlfC 12.79 2.63 4.86 ↵a Tranglycolylation/hydrolysis (Vtrans/Vhyd) ratios were calculated from the initials rates of formation of transglycosylation products over the initial rates of hydrolysis.
