Jump to content

Spermine synthase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Karthi.dr (talk | contribs) at 03:42, 30 September 2022 (Copyedit). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Spermine synthase
Identifiers
EC no.2.5.1.22
CAS no.74812-43-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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. 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.