The recent breakthrough in all-atom, protein structure prediction opens new avenues for a range of computational approaches in enzyme design. These new approaches could become instrumental for the development of technical biocatalysts, and hence our transition toward more sustainable industries. Here, we discuss one approach, which is well-known within inorganic catalysis, but essentially unexploited in biotechnology. Specifically, we review examples of linear free-energy relationships (LFERs) for enzyme reactions and discuss how LFERs and the associated Sabatier Principle may be implemented in algorithms that estimate kinetic parameters and enzyme performance based on model structures. •Linear scaling between binding- and activation energies occurs for some enzyme reactions.•This is particularly seen for heterogeneous biocatalysis involving insoluble substrate.•Linear free-energy relationships simplify computational prediction of kinetic parameters.•It is proposed that this can be exploited in future enzyme discovery and -engineering.