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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The nearly ubiquitous polyamines (putrescine, spermidine and spermine) are polycationic mediators of cell proliferation and differentiation whose functions likely provide both stability and neutralisation for nucleic acids. The following polyamine biosynthetic enzymes are evolutionary related [ ]:Spermidine synthase ( ) (putrescine aminopropyltransferase). It catalyses the last step in the biosynthesis of spermidine from arginine and methionine; the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor. Spermine synthase ( ) (spermidine aminopropyltransferase). It converts spermidine into spermine using decarboxylated S-adenosylmethionine as the cofactor. Putrescine N-methyltransferase ( ). It catalyzes a step in the biosynthesis of nicotine in plants; the methylation of putrescine to N- methylputrescine using S-adenosylmethionine as the cofactor.The Thermotoga maritima spermidine synthase monomer consists of two domains: an N-terminal domain composed of six β-strands, and a Rossmann-like C- terminal domain. The larger C-terminal catalytic core domain consists of a seven-stranded β-sheet flanked by nine α-helices. This domain resembles a topology observed in a number of nucleotide and dinucleotide-binding enzymes, and in S-adenosyl-L-methionine (AdoMet)- dependent methyltransferase (MTases) [ ]. | Name | Spermidine/spermine synthases |
| Short Name | Spermi_synthase | Type | Family |
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