+ S-adenosyl
methioninamine
Thermospermine synthase
| Thermospermine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.79 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Thermospermine synthase (EC 2.5.1.79, TSPMS, ACL5 (ACAULIS5), SAC51) is an enzyme characterised from Thalassiosira pseudonana and Arabidopsis thaliana with systematic name S-adenosylmethioninamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing).[1] It catalyses a chemical reaction in which an aminopropyl group is transferred from the coenzyme, S-adenosylmethioninamine to spermidine, giving thermospermine:[2][3]
This enzyme is required for correct xylem specification through regulation of the lifetime of the xylem elements.[4]
References
- ↑ Enzyme 2.5.1.79 at KEGG Pathway Database.
- ↑ Romer P, Faltermeier A, Mertins V, Gedrange T, Mai R, Proff P (November 2008). "Investigations about N-aminopropyl transferases probably involved in biomineralization". Journal of Physiology and Pharmacology. 59 Suppl 5: 27–37. PMID 19075322.
- ↑ Knott JM, Römer P, Sumper M (June 2007). "Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine". FEBS Letters. 581 (16): 3081–6. Bibcode:2007FEBSL.581.3081K. doi:10.1016/j.febslet.2007.05.074. PMID 17560575.
- ↑ Muñiz L, Minguet EG, Singh SK, Pesquet E, Vera-Sirera F, Moreau-Courtois CL, Carbonell J, Blázquez MA, Tuominen H (August 2008). "ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death". Development. 135 (15): 2573–82. doi:10.1242/dev.019349. PMID 18599510.
External links
- Thermospermine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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