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Zum Mechanismus derβ-Lysin-Mutase-Reaktion
Authors:J Rétey  F Kunz  T C Stadtman  D Arigoni
Institution:(1) Organisch-chemisches Laboratorium der Eidg. Technischen Hochschule, Zürich, Schweiz;(2) The Laboratory of Biochemistry, Section on Enzymes, National Heart Institute, National Institutes of Health, Bethesda, Maryland, USA
Abstract:Summary Using tritium labelled substrates it is shown that in the rearrangement of (S) -beta-lysine to 3,5-diaminohexanoic acid catalysed bybeta-lysine mutase a stereospecific hydrogen migration from C-5 to C-6 of the substrate occurs. When the reaction is carried out in the presence of 5prime-3H]-coenzyme B12, the heavy isotope is transferred both to C-6 of 3, 5-diaminohexanoate and to C-5 ofbeta-lysine. In the latter the labelled atom occupies the same diastereotopic position as the H atom that is transferred to C-6 of the product.
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