Fig. 1: Model system based on P450BM3 as biocatalyst for the selective oxidation of a steroidal substrate. | Nature Communications

Fig. 1: Model system based on P450BM3 as biocatalyst for the selective oxidation of a steroidal substrate.

From: Pervasive cooperative mutational effects on multiple catalytic enzyme traits emerge via long-range conformational dynamics

Fig. 1

a Testosterone (1) is selectively hydroxylated at position 2β (2) by mutant III (R47I/T49I/Y51I/F87A). b Active site of parent enzyme showing F87A mutation (black) above the haem (yellow) as well as WT resides R47, T49 and Y51 (red). The distances between the α-C atoms of the following pairs of residues are (Å): R47-T49 (7.0), R47-Y51 (13.4), T49-Y51 (7.0). Image and atom distances calculations obtained with PyMol Molecular Graphics System, V. 1.5.0.4 (Schrödinger, LLC). An interactive figure of parental variant --- docked with 1 was created with Michelanglo68 (https://michelanglo.sgc.ox.ac.uk/r/p450) highlighting the mutated residues and secondary structures discussed in this work. c The 6 possible evolutionary trajectories between parental mutant F87A (---) and “triple” mutant III involve three “single” mutants I-- (R47I/F87A), -I- (T49I/F87A) and --I (Y51I/F87A) as well as three “double” mutants II- (R47I/T49I/F87A), I-I (R47IY51I/F87A) and -II (T49I/Y51I/F87A). d Mutant abbreviations. The signs − and + indicate that the respective mutation is absent and present, respectively.

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