Disease relevance of C06366

• The homospermidine synthase encoding cDNA was subcloned into the expression vector pet15b and overexpressed in E. coli [1].
• Sequence analysis of the 330-kb genome of chlorella virus Paramecium bursaria chlorella virus 1 (PBCV-1) revealed an open reading frame, A237R, that encodes a protein with 34% amino acid identity to homospermidine synthase from Rhodopseudomonas viridis [2].
• All the cyanobacteria capable of fixing nitrogen, contained sym-homospermidine as the major polyamine [3].
• Flavobacterium complex and green bacteria contain putrescine and homospermidine [4].
• Purification and characterization of homospermidine synthase in Acinetobacter tartarogenes ATCC 31105 [5].

High impact information on C06366

• Thus it was found that [14C]putrescine can replace eIF5A precursor protein as an acceptor of the 4-aminobutyl moiety of spermidine to form radiolabeled homospermidine [6].
• Sequence comparisons of the two enzymes indicate an evolutionary origin of homospermidine synthase from ubiquitous deoxyhypusine synthase [7].
• We further find no evidence for the ability of PAO to metabolize the secondary amine position in homospermidine, which is devoid of such complicating side reactions [8].
• Bacteroids, isolated from root nodules, contained both sym-homospermidine and 4-aminobutylcadaverine, whereas the plant cytosol fraction contained large quantities of putrescine and cadaverine [9].
• The enzyme homospermidine synthase catalyzes the NAD+-dependent conversion of 2 mol putrescine into homospermidine [1].

Chemical compound and disease context of C06366

• Structural specificity of the triamines sym-homospermidine and aminopropylcadaverine in stimulating growth of spermidine auxotrophs of Escherichia coli [10].
• In the order Thermales, Thermus and Marinithermus contained homospermidine, norspermine and the linear penta-amines [11].

Biological context of C06366

• Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein [7].
• N4-Benzyl-N1,N8-bis[[2-(2-hydroxyphenyl)thiazolin-4-yl]carbonyl] homospermidine (5) proved to be the most potent antiproliferative and cytocidal compound in the series with in vitro IC50 values of 3 and 1 microM on L1210 and P388 murine cell lines [12].
• Crystal and molecular structure of sym-homospermidine monohydrate [13].

Anatomical context of C06366

• The polyamine pattern consisted of sym-homospermidine as the major compound. meso-Diaminopimelic acid was found as the characteristic cell-wall diamino acid [14].
• Cadaverine was detected only in amphibian testes; sym-homospermidine was found not only in testes but also in various other tissues of amphibians and of some reptiles [15].

Associations of C06366 with other chemical compounds

• In conclusion, homospermidine synthase behaves like a deoxyhypusine synthase that lost its major function (aminobutylation of eIF5A precursor protein) but retained unaltered its side activity (aminobutylation of putrescine) [7].
• Appreciable amounts of spermine and sym-homospermidine were detected only in the species belonging to the Rhodophyta (red algae) [16].
• Since the diamine putrescine is a precursor of homospermidine and nicotine in tobacco, we performed heterologous expression of a bacterial homospermidine synthase gene (hss)in Nicotiana tabacum and determined the effect on free and conjugated polyamine levels [17].

Gene context of C06366

• Currently research on spermidine metabolism is based on the deposition of the deoxyhypusine synthase nucleic acid sequence in GenBank while the activity of homospermidine synthase was deduced from inhibitor studies [18].

Analytical, diagnostic and therapeutic context of C06366

• Purification, molecular cloning and expression in Escherichia coli of homospermidine synthase from Rhodopseudomonas viridis [19].

References