Most of the compounds have physiologically active properties, and their biological properties are often attributed to the heteroatoms contained in their molecules, and most of these heteroatoms also appear in cyclic structures. A Journal, Comparative Study, Article, Biochemical Pharmacology called Putrescine or spermidine binding site of aminopropyltransferases and competitive inhibitors, Author is Shirahata, Akira; Morohohi, Toru; Fukai, Masayo; Akatsu, Sakae; Samejima, Keijiro, which mentions a compound: 35621-01-3, SMILESS is NC1CCNCC1.[H]Cl.[H]Cl, Molecular C5H14Cl2N2, Related Products of 35621-01-3.
A model of the active site of aminopropyltransferases was proposed based on the study of a number of monoamino and diamino compounds as potential inhibitors and substrates, resp., of spermidine synthase purified from pig liver. The active site seems to have a relatively large hydrophobic cavity adjacent to a neg. charged site, to which a protonated amino group of putrescine binds, with another amino group of putrescine being situated in the hydrophobic cavity as a free form to be aminopropylated by decarboxylated S-adenosylmethionine. On the basis of the above-mentioned model, another modified one was proposed for spermine synthase, and several compounds designed according to the modified model were found to potently inhibit spermine synthase, purified from rat brain, in competition with spermidine. The newly developed inhibitors were about two orders of magnitude more potent in vitro than a known inhibitor of spermine synthase, dimethyl(5′-adenosyl)sulfonium perchlorate.
Although many compounds look similar to this compound(35621-01-3)Related Products of 35621-01-3, numerous studies have shown that this compound(SMILES:NC1CCNCC1.[H]Cl.[H]Cl), has unique advantages. If you want to know more about similar compounds, you can read my other articles.
Reference:
Pyrimidine | C4H4N2 – PubChem,
Pyrimidine – Wikipedia