Fig. 4: Investigating the structural basis of MBH reaction catalyzed by GkOYE.8. | Nature Communications

Fig. 4: Investigating the structural basis of MBH reaction catalyzed by GkOYE.8.

From: Unlocking the function promiscuity of old yellow enzyme to catalyze asymmetric Morita-Baylis-Hillman reaction

Fig. 4

a The dimer architecture of apo-GkOYE.8 shown as surface pattern and cartoon pattern. b Structure alignment of GkOYE (PDB ID: 3gr7) and apo-GkOYE.8 (PDB ID: 8X0J). GkOYE shown as green, apo-GkOYE.8 shown as pink. c Determination of stereoselectivities of GkOYE.7 and GkOYE.8. d The architecture of the complex form of GkOYE.8-3 and the key residues within a 4 Å radius. e The results of the alanine scan. f The results of C26 sites saturation mutation. g The results of H164 sites saturation mutation. n = 3 independent biological experiments. Data are presented as mean values ± SD. Source data are provided as a Source Data file.

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