Fig. 2: Multiple enzymatic parameters of deconvolution mutants. | Nature Communications

Fig. 2: Multiple enzymatic parameters of deconvolution mutants.

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

Fig. 2

a Selectivity and conversion data are obtained from HPLC data and shown in percentage. b NADPH leak and consumption rate were measured in the absence and presence of testosterone (1) substrate, respectively. c Product formation rate (PFR) is calculated by multiplying the NADPH consumption rate by coupling efficiency. d Coupling efficiency (CE) is the ratio between NADPH consumption and production formation, and it is reported in percentage. e TTN describes the total moles of products per moles of enzyme after NADPH depletion. f TTF normalizes TTN by time after NADPH depletion. See Fig. 1d for mutant abbreviations. Other products mainly include the 15β-alcohol and other regioisomers. The data represent the average of two independent experiments (n = 2). Source data are provided with this paper.

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