Fig. 7: Relationship between \({K}_{m}\) and \([{{{{{\rm{S}}}}}}]\) from the dataset reported by Park et al.42. | Nature Communications

Fig. 7: Relationship between \({K}_{m}\) and \([{{{{{\rm{S}}}}}}]\) from the dataset reported by Park et al.42.

From: Thermodynamic principle to enhance enzymatic activity using the substrate affinity

Fig. 7

The raw values of \({K}_{m}\) and \([{{{{{\rm{S}}}}}}]\) are shown in a, and their relative values are plotted in b. Each entry of \({K}_{m}\) and \([{{{{{\rm{S}}}}}}]\) was categorized based on the number of times the substrate appeared in the entire dataset. Red: <50 (major metabolites), blue: > 50 (NAD+, NADH, NADP+, NADPH, and acetyl-CoA), black: > 300 (ATP). The number of entries was used as a proxy for the validity of the Michaelis-Menten mechanism of the specific substrate. The dashed line in a corresponds to \({K}_{m}=[{{{{{\rm{S}}}}}}]\), and the shaded area shows a deviation of 1 order of magnitude.

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