57672-23-8Relevant articles and documents
1,5-DIAZABICYCLONONANE, THE OXIDATION PRODUCT OF SPERMINE
Croker, S. J.,Loeffler, R. S. T.,Smith, T. A.,Sessions, R. B.
, p. 1559 - 1560 (1983)
The structure of the product of the chemical or enzymatic oxidation of spermine was shown to be 1,5-diazabicyclononane (III).
Biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases
Galman, James L.,Slabu, Iustina,Weise, Nicholas J.,Iglesias, Cesar,Parmeggiani, Fabio,Lloyd, Richard C.,Turner, Nicholas J.
supporting information, p. 361 - 366 (2017/08/14)
The discovery and characterisation of enzymes with both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals.
Site Selective and Quantitative C-N Bond Cleavage of Spermine on a Cobalt Complex
Yashiro, Morio,Mori, Tomonori,Sekiguchi, Makoto,Yoshikawa, Sadao,Shiraishi, Shinsaku
, p. 1167 - 1168 (2007/10/02)
A C-N bond of spermine coordinated to cobalt(II) is cleaved through site-selective oxidation to yield 1,5-diazabicyclononane and complexes containing 1,3-diaminopropane in an aqueous solution.
