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doi: 10.1186/s12929-020-00679-2 122 ToledoM

Mankiewicz et al., 2022) although the mechanisms may be different

Interconversion of AAT and TAT The rapid increase in the availability of amino acid sequences for enzymes in the last ~15 years has spurred an interest in being able to predict, from comparisons of amino acid conservation patterns, the positions in structurally homologous enzymes that determine reaction and substrate specificity differences.[88] Our interests in this area originated in attempts to convert GABA aminotransferase into a decarboxylase.[89, 90] Our frustrating failures based on manual analysis of multiple sequence alignments and chemists intuition led us to devise a statistical method for extracting this information.[91] Over the course of developing the program (named JANUS) several other groups developed programs with similar goals, but ours has the following unique features: it employs a direct comparison of two enzymes (the starting point and target of conversion), it employs an amino acid distance (substitution) matrix based on a principle component analysis of 237 amino acid physicochemical properties, it accounts for both structural conservation and covariation, and it was experimentally validated using AAT-to-TAT as an example