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 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.
This biochemistry article is a stub.