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Among the over 50 gyrate atrophy‐causing mutations of ornithine δ‐aminotransferase (OAT), the R180T involves an active site residue located at the dimer interface, which in the crystal structure of OAT complexed with 5‐fluoromethylornithine engages a salt bridge with the α‐carboxylate of the substrate analogue. Starting from the previous finding that no transaminase activity was detected in CHO‐K...
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