Figure 3: Active site of AmyPΔSBD. | Scientific Reports

Figure 3: Active site of AmyPΔSBD.

From: Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13

Figure 3

(a) Electron density of maltotriose bound to the active site of the E221Q mutant of AmyPΔSBD from the 2Fo–Fc map contoured at 2σ in the AmyP-E221Q/γ-CD structure. Glucose residues in the oligosaccharide are numbered from the non-reducing end. His129 is from domain B (magenta). Hydrogen bonds are shown as dashed lines. (b) Electron density of maltose bound to the active site of WT AmyPΔSBD from the 2Fo–Fc map contoured at 2σ in the AmyP/β-CD structure. Glucose residues in the oligosaccharide are numbered from the non-reducing end. (c) Time-course analysis of the hydrolysis products of the γ-CD substrate produced by WT AmyPΔSBD and its Y36A mutant, respectively, using TLC. Std, standards.

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