Figure 5 | Scientific Reports

Figure 5

From: Semi-rational engineering of a thermostable aldo–keto reductase from Thermotoga maritima for synthesis of enantiopure ethyl-2-hydroxy-4-phenylbutyrate (EHPB)

Figure 5The alternative text for this image may have been generated using AI.

The optimal (S)-EHPB- and (R)-EHPB-preferring Tm1743 double mutants and models of their EOPB binding conformations. (a) The percentage of (S)-EHPB (green) and (R)-EHPB (salmon) produced by different Tm1743 double mutants. (b) and (c) Stereo views of the EOPB binding models of the best (S)-EHPB-preferring (W21L/W118H) and (R)-EHPB-preferring (W21S/W86E) mutants. Amino acids involved in EOPB coordination are shown as gray sticks, and the pro-S and pro-R conformations of EOPB are colored green and salmon, respectively. NADPH is shown as orange sticks.

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