Zum Mechanismus derβ-Lysin-Mutase-Reaktion |
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Authors: | J Rétey F Kunz T C Stadtman D Arigoni |
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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 |
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Abstract: | Summary Using tritium labelled substrates it is shown that in the rearrangement of (S) --lysine to 3,5-diaminohexanoic acid catalysed by-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 5-3H]-coenzyme B12, the heavy isotope is transferred both to C-6 of 3, 5-diaminohexanoate and to C-5 of-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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