Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous

@article{Neidhart1990MandelateRA,
  title={Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous},
  author={David J. Neidhart and George L. Kenyon and John A. Gerlt and Gregory A. Petsko},
  journal={Nature},
  year={1990},
  volume={347},
  pages={692-694}
}
MANDELATE racemase (MR) and muconate lactonizing enzyme (MLE) catalyse separate and mechanistically distinct reactions necessary for the catabolism of aromatic acids by Pseudomonas putida1–3. The X-ray crystal structure of MR, solved at 2.5 Å resolution, reveals that the secondary, tertiary and quaternary structures of MR and MLE4 are remarkably similar; also, MR and MLE are about 26% identical in primary structure5. However, MR has no detectable MLE activity and vice versa. Thus, MR and MLE… 
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Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues.
TLDR
A model of a productive substrate complex of MR has been constructed on the basis of difference Fourier analysis at 3.5-A resolution of a complex between MR and (R,S)-p-iodomandelate, permitting identification of residues that may participate in substrate binding and catalysis.
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