MECHANISM OF BETA-LYSINE-MUTASE REACTION

Using tritium labelled substrates it is shown that in the rearrangement of (S) -β-lysine to 3,5-diaminohexanoic acid catalysed by β-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 β-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. © 1969 Birkhäuser Verlag.