Cadaverine distribution

Decodine derived from [l-14C]cadaverine showed a distribution of label identical to that of the lysine-derived samples. Activity was equally divided between C-9 (j8-alanine) and C-5 (2-piperydylacetate minus -alanine). In decodine, into which AC - Cjpiperideine was incorporated, the label was confined to C-9. This was consistent with the established evidence that the double bond in A -piperideine does not migrate from one side of the nitrogen to the other (89, 90). 

If the former, only two carbons would be radioactive. Degradation, however, showed that radioactivity was equally distributed between all four C-atoms—2, 6, 10, and 11. Consequently, in this case at least, cadaverine is a metabolic intermediate. 

Administration of both lysine-2- C and lysine-6- C led to the formation of labeled lycopodine. Degradation showed that approximately 25% of the label was located at C-5 (isolated as benzoic acid) and 25% at C-9 (isolated as formic acid). The remainder was assumed to be at C-1 (25%) and C-13 (25%) and although neither C-1 nor C-13 was isolated individually it was possible to obtain C-9 in conjunction with C-13 as 7-methyltetrahydroquinoline. This fragment contained approximately 50% of the activity of lycopodine. These results are compatible with the incorporation of two five-carbon chains derived from lysine into the lycopodine skeleton but they indicate that, unlike the incorporation of lysine into A-methylpelletierine shown in Scheme 4, the incorporation proceeds via a symmetrical intermediate. Next it was found that cadaverine-l- C was incorporated into lycopodine and gave the same distribution of activity as lysine. Thus it was likely that cadaverine was the symmetrical intermediate on the pathway from lysine to pelletierine. These findings are incorporated into Scheme 7 in which lysine-6- C is used as an example but the same distribution of activity would also apply to lysine-2- C. This scheme for the incorporation of lysine was supported by experiments with a doubly labeled lysine, 4,5- H2-6- C-lysine. 

Diamine Oxidase. The original description of the enzyme that oxidizes diamines was based on the oxidation of histamine, and the enzyme was named histaminase. The name diamine oxidase was applied when evidence was obtained that the same enzyme also attacks cadaverine, putres-cine, and agmatine. This activity has also been found widely distributed among animals, plants, and microorganisms. ... 

Polyamines, such as spermine, spermidine, putrescine, cadaverine, are natural substances widely distributed in vegetable, animal and bacterial cells. They enter in the composition of bacterial viruses. They have a wide range of effects, but they are difficult to localize within the cell and their physiological significance is not understood very well. In animal cells and sera there exists a diamineoxidase which converts spermine into highly cytotoxic compounds, and many effects seen in tissue cultures are attributed to these substances. 

Apart from aminoacids, peptides and proteins, many other metalbinding substances play essential roles in all living cells. Firstly, there are the pteridines (including folic acid) and purines, whose stability constants have been determined (Albert, 1953 Albert and Serjeant, 1960).Riboflavine is most avid in the partly reduced state (Hemmerich, Veeger and Wood, 1965). Spermine (//. ), and the simpler diamines such as spermidine and cadaverine, are widely distributed metal-binders. 

Crystals of spermine phosphate were first seen by van Leeuwenhoek (1678) in human semen. Since then several other di- and polyamines have been discovered in both prokaryotes and eukaryotes. It now seems probable that putrescine and spermidine are biologically ubiquitous. In general, prokaryotes have a higher concentration of putrescine than spermidine, and lack spermine. Eukaryotes, on the other hand, usually have little putrescine, but high concentrations of spermidine and spermine. Cadaverine, which normally arises from decarboxylation of lysine, has a limited occurrence and its distribution has not... 

---