Biology:Spermine synthase

From HandWiki

Spermine synthase (EC 2.5.1.22, spermidine aminopropyltransferase, spermine synthetase) is an enzyme that converts spermidine into spermine.[1][2] This enzyme catalyses the following chemical reaction

S-adenosylmethioninamine + spermidine [math]\displaystyle{ \rightleftharpoons }[/math] S-methyl-5'-thioadenosine + spermine

Spermine synthase is an enzyme involved in polyamine biosynthesis. It is present in all eukaryotes and plays a role in a variety of biological functions in plants[3] Its structure consists of two identical monomers of 41 kDa with three domains each, creating a homodimer formed via dimerization. The interactions between one of the three domains, the N-terminals of the monomers, is responsible for dimerization as that is where the active site is located; the central terminal consisting of four β- strands structurally forming a lid for the third domain, the C-terminal domain.[4]

References

  1. "Studies of inhibition of rat spermidine synthase and spermine synthase". The Biochemical Journal 187 (2): 419–28. May 1980. doi:10.1042/bj1870419. PMID 7396856. 
  2. "Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain". European Journal of Biochemistry 101 (2): 619–26. November 1979. doi:10.1111/j.1432-1033.1979.tb19756.x. PMID 520313. 
  3. "Characterization of spermidine synthase and spermine synthase--The polyamine-synthetic enzymes that induce early flowering in Gentiana triflora". Biochemical and Biophysical Research Communications 463 (4): 781–6. August 2015. doi:10.1016/j.bbrc.2015.06.013. PMID 26056006. 
  4. "Spermine synthase". Cellular and Molecular Life Sciences 67 (1): 113–21. January 2010. doi:10.1007/s00018-009-0165-5. PMID 19859664. 

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