A) HisA and TrpF catalyze Amadori rearrangements of structurally different substrates. B) The ProFAR substrate in the active site of the catalytically inactive D7N D176A HisA (PDB 5A5W). C) A TrpF product analog, rCdRP (reduced 1′-(2′-carboxyphenylamino)-1′-deoxyribulose 5′-phosphate), positioned in the active site of HisA(D7N/dup13–15/D10G) based upon its position in the active site of the ortholog PriA (PDB 2Y85). Reprinted with permission from Proc Natl Acad Sci USA
114(18):4727–32, 2017. Structural and functional innovations in the real-time evolution of new (betaalpha)8 barrel enzymes. Newton MS, Guo X, Soderholm A, Nasvall J, Lundstrom P, Andersson DI, et al.