Spermine synthase (, ''spermidine aminopropyltransferase'', ''spermine synthetase'') is an enzyme that converts

spermidine Spermidine is a polyamine compound () found in ribosomes and living tissues and having various metabolic functions within organisms. It was originally isolated from semen. Function Spermidine is an aliphatic polyamine. Spermidine synthase (SPDS ...

into

spermine Spermine is a polyamine involved in cellular metabolism that is found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid ornithine. It is an essential growth factor in some bacteria as well. It is found as a po ...

. This enzyme catalyses the following

chemical reaction A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and break ...

S-adenosylmethioninamine ''S''-Adenosylmethioninamine is a substrate that is required for the biosynthesis of polyamines including spermidine, spermine, and thermospermine. It is produced by decarboxylation of ''S''-adenosyl methionine. See also * Adenosylmethionin ...

\rightleftharpoons

S-methyl-5'-thioadenosine +

Spermine synthase is an enzyme involved in

polyamine A polyamine is an organic compound having more than two amino groups. Alkyl polyamines occur naturally, but some are synthetic. Alkylpolyamines are colorless, hygroscopic, and water soluble. Near neutral pH, they exist as the ammonium derivatives. ...

biosynthesis. It is present in all

eukaryote Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bact ...

s and plays a role in a variety of biological functions in plants Its structure consists of two identical

monomer In chemistry, a monomer ( ; ''mono-'', "one" + '' -mer'', "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization. Classification ...

s of 41 kDa with three domains each, creating a

homodimer In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has ...

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.

References

External links

* * * EC 2.5.1 {{Biochem-stub