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Fig. 4 | BMC Evolutionary Biology

Fig. 4

From: Insights into the evolution of enzyme substrate promiscuity after the discovery of (βα)8 isomerase evolutionary intermediates from a diverse metagenome

Fig. 4

Comparison of steady-state enzyme kinetics. A graphical comparison of the catalytic efficiencies (k cat /K M) of wild type and mutant enzymes that were characterized is shown. Values for ProFAR (x axis) and PRA (y axis) isomerase activities, expressed as log10, are compared. Data from HisA_Afer (red square), PriA_Blon (blue circle), CAM1 (green circle), CAM1_A81S (green circle with a black border and inner black circle) and CAM1_A81G (green circle with a black border and inner black cross, this study), as well as from PriA_Scoe (blue circle) and the Ser81Thr mutant of PriA from S. coelicolor, labeled as PriA_Scoe (blue circle with a black border and inner black circle) (data obtained from [38]), is included

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