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- W2093564207 abstract "Investigations on the β-lysine mutase reaction: Mechanism and steric course The steric course and some mechanistic aspects of the coenzyme-B12-dependent β-lysine-mutase reaction, in which (3 S)-β-lysine is converted to (3 S, 5 S)-3, 5-diaminohexanoate, have been investigated by means of tritium labelling. The reaction involves migration of an hydrogen atom from C(5) of the substrate to C(5′) of coenzyme B12 and back-transfer to C(6) of the product. In the presence of [5′-3H]-coenzyme B12 the enzyme catalyzes the exchange of label between the cofactor and one of the diastereotopic H-atoms at C(5) of the substrate. The exchangeable hydrogen atom is identical with the one specifically involved in the migration reaction. Degradation of the tritiated β-lysine obtained in such experiments yielded a sample of tritiated succinic acid which was shown in an enzymic assay involving partial oxidation with succinate dehydrogenase, to possess the (S)-configuration. Thus, the overall substitution at C(5) occurs with inversion of configuration." @default.
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- W2093564207 date "1978-12-13" @default.
- W2093564207 modified "2023-10-06" @default.
- W2093564207 title "Zur Kenntnis der β-Lysin-Mutase-Reaktion: Mechanismus und sterischer Verlauf" @default.
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- W2093564207 doi "https://doi.org/10.1002/hlca.19780610824" @default.
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