Fig. 3
From: Constructing a synthetic pathway for acetyl-coenzyme A from one-carbon through enzyme design
Protein engineering and mechanism analysis of the glycolaldehyde synthase. a Kinetic parameters of WT and mutants. WT: wild type; M1: mutations at W86R and N87T; M2: mutations at W86R, N87T, L109G, and L110E; M3: mutations at W86R, N87T, L109G, L110E and A460M; M4: mutations at W86R, N87T, L109G, L110E, A460M, H281V, and Q282F. b The overview of the selected five mutations in active center. IMA: intermediate analogue; the orange lines indicate the hydrogen bonds between the hydroxyl group of IMA and the mutation L110E. c The pocket volumes of M1, M2, M3, and M4. Pink dots represent the volumes of the binding-pockets (Supplementary Data 2), which are 131.25, 161.50, 133.38, and 171.38 Å3, respectively. The figures were rendered using UCSF Chimera software version 1.1246. Source data are provided as a Source Data file.
