Spermine synthase
Identifiers
EC no.2.5.1.22
CAS no.74812-43-4
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IntEnzIntEnz view
BRENDABRENDA entry
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MetaCycmetabolic pathway
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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 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. ↑ Hibasami H, Borchardt RT, Chen SY, Coward JK, Pegg AE (May 1980). "Studies of inhibition of rat spermidine synthase and spermine synthase". The Biochemical Journal. 187 (2): 419–28. doi:10.1042/bj1870419. PMC 1161808. PMID 7396856.
  2. ↑ Pajula RL, Raina A, Eloranta T (November 1979). "Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain". European Journal of Biochemistry. 101 (2): 619–26. doi:10.1111/j.1432-1033.1979.tb19756.x. PMID 520313.
  3. ↑ Imamura T, Fujita K, Tasaki K, Higuchi A, Takahashi H (August 2015). "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. doi:10.1016/j.bbrc.2015.06.013. PMID 26056006.
  4. ↑ Pegg AE, Michael AJ (January 2010). "Spermine synthase". Cellular and Molecular Life Sciences. 67 (1): 113–21. doi:10.1007/s00018-009-0165-5. PMC 2822986. PMID 19859664.
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