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  • Title: Stereochemistry of proton abstraction catalyzed by lysine and ornithine omega-aminotransferases.
    Author: Tanizawa K, Yoshimura T, Asada Y, Sawada S, Misono H, Soda K.
    Journal: Biochemistry; 1982 Mar 02; 21(5):1104-8. PubMed ID: 6280755.
    Abstract:
    (6R)-L-[6-3H]Lysine and (6S)-L-[6]3H]lysine were prepared to investigate the stereochemical aspects of the reaction catalyzed by bacterial L-lysine epsilon-aminotransferase. When (6R)-L-[6-3H]lysine was used as a substrate, the tritium label was retained in the product, delta 1-piperideine-6-carboxylate. In contrast, the radioactivity from (6S)-L-[6-3H]lysine was found in the solvent. Thus, the pro-S hydrogen at the prochiral C-6 carbon of L-lysine is specifically abstracted by L-lysine epsilon-aminotransferase. The proton exchange was observed by proton nuclear magnetic resonance analysis in the reaction of bacterial L-ornithine delta-aminotransferase with L-ornithine in 2H2O. The isolated L-[5-2H]ornithine was converted to dextrorotatory 4-phthalimido[4-2H]butyrate. This indicates that L-ornithine delta-aminotransferase catalyzes the stereospecific exchange of the pro-S hydrogen at the prochiral C-5 carbon of L-ornithine with the solvent.
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