Abstract
IT has been shown previously in experiments with crude glutamic aminopherase, α-deuterio-alanine and α-ketoglutarate that enzymatic transamination involves dissociation of the α-hydrogen of the original amino-acid and its replacement, in the newly formed amino-acid, by a hydrogen ion derived from the aqueous medium1. In the non-enzymatic transamination reaction of Herbst, associated with de-carboxylation of the NH2-donating amino-acid, there occurs no dislocation of labelled α-hydrogen (Herbst and Rittenberg2). The reaction mechanisms have been discussed by Herbst3 and Braun-stein4.
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References
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KONIKOVA, A., DOBBERT, N. & BRAUNSTEIN, A. Labilization of the α-Hydrogen of Amino-acids in the Presence of Aminopherase. Nature 159, 67–68 (1947). https://doi.org/10.1038/159067a0
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DOI: https://doi.org/10.1038/159067a0
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