Selective oxidation of testosterone by P450 BM3
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Description
In the manuscript 'Pervasive cooperative mutational effects on multiple catalytic enzyme traits emerge via long-range conformational dynamics .' the following structural features are discussed a-A loop, A helix, B helix, B-B' loop, β4 sheet, F-G loop, G helix.
Along with testosterone and the cofactor is heme, several residues are discussed: R47, T49, Y51 and F87A.
Model system
Model system based on P450 BM3 as biocatalyst for the selective oxidation of a steroidal substrate.
Testosterone is selectively hydroxylated at position 2β in the current representation. Active site of parental mutant F87A highlighting residues most likely involved in regio- and diastereoselectivity. 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).
There are 6 possible evolutionary trajectories between parental mutant F87A (---) and “triple” mutant (R47I/T49I/Y51I/F87A; III). Click on a circle to load it.