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This BtrG/GCT fold distinguishes these enzymes from others exhibiting cyclotransferase-like activity ( Bioinformatic analysis has identified a diverse set of residues that are critical for CHAC1 activity and collectively form its active site ( 38 YGSL 41 , D 68 , R 72 , E 115 and Y 143 are responsible for high affinity substrate binding via salt bridge interaction with the glutamate (E 115 ), hydrogen bonding as well as a cation -interaction involving Y 143