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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