LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | The nearly ubiquitous polyamines (putrescine, spermidine and spermine) are polycationic mediators of cell proliferation and differentiation whosefunctions likely provide both stability and neutralisation for nucleic acids. The following polyamine biosynthetic enzymes are evolutionary related []:Spermidine synthase ( ) (putrescine aminopropyltransferase). It catalyzes the last step in the biosynthesis of spermidine from arginine andmethionine; 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-adenosylmethionineas 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 domainconsists of a seven-stranded β-sheet flanked by nine α-helices. This domain resembles a topology observed in a number of nucleotide anddinucleotide-binding enzymes, and in S-adenosyl-L-methionine (AdoMet)- dependent methyltransferase (MTases) []. |
| Short Name | Spermi_synthase |
