Fig. 2: Substrate binding and chemoselectivity. | Nature Communications

Fig. 2: Substrate binding and chemoselectivity.

From: Coordinated conformational changes in P450 decarboxylases enable hydrocarbons production from renewable feedstocks

Fig. 2: Substrate binding and chemoselectivity.

Representation of superimposed OleTPCL structure with the CYP152 decarboxylases OleTKM (a), OleTPRN [PDB: 8D8P] (b) and OleTJE [PDB: 4L40] (c), and the hydroxylases P450BSβ [PDB: 1IZO] (d), P450BM [PDB: 6FYJ] (e) and P450SPα [PDB: 3AWM] (f), showing substrate and canonical histidine and phenylalanine (and valine/leucine) positioning in the binding pockets. g Product yield of turnover reactions performed with OleTPCL wildtype (WT) and V86F and H92Q mutants with different FA substrates. Lighter, medium, and darker bar colors stand for alkene, α-hydroxy- and β-hydroxy-fatty acid, respectively. Results represent the mean and standard deviation of three independent experiments (n = 3).

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