Engineering substrate promiscuity in halophilic alcohol dehydrogenase (HvADH2) by in silico design
Fig 5
Docking of (R)-1-PheOH (white spheres).
A) Catalytic site of the WT enzyme (F85 and F108 green spheres, NAD+, yellow sticks) shows stabilization of the substrate aromatic ring by F108. The distance from the hydroxyl oxygen to the catalytic zinc (O-Zn) is 4.6 Å, and the distance from the substrate α-carbon to the C4 of the nicotinamide ring (αC-C4), is 5.7 Å. B) Catalytic site of the F108G variant. The distance from the hydroxyl oxygen to the catalytic zinc (O-Zn) is 2.5 Å, and the distance from the substrate α-carbon to the C4 of the nicotinamide ring (αC-C4), is 4.0 Å.