Nicotianamine synthase
| nicotianamine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.43 | ||||||||
| CAS no. | 161515-44-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a nicotianamine synthase (EC 2.5.1.43) is an enzyme that catalyzes the chemical reaction
- 3 S-adenosyl-L-methionine 3 S-methyl-5'-thioadenosine + nicotianamine
Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, S-methyl-5'-thioadenosine and nicotianamine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-Lmethioni ne 3-amino-3-carboxypropyltransferase.
References
[edit]- Higuchi K, Kanazawa K, Nishizawa NK, Chino M, Mori S (1994). "Purification and characterization of nicotianamine synthase from Fe-deficient barley root". Plant Soil. 165 (2): 173–179. doi:10.1007/BF00008059.
