Tricin synthase
| Tricin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.175 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tricin synthase (EC 2.1.1.175, ROMT-17, ROMT-15, HvOMT1, ZmOMT1) is an enzyme with systematic name S-adenosyl-L-methionine:tricetin 3',5'-O-dimethyltransferase.[1][2] This enzyme catalyses the following overall chemical reaction
The enzyme adds two methyl groups, in sequence, to the flavone tricetin. The first goes on one of the ortho positions in the ring which has three phenolic oxygens, followed by the other, to give tricin. The methyl groups come from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Oryza sativa (ROMT-15 and ROMT-17).[3]
See also
- Tricetin 3',4',5'-O-trimethyltransferase, an enzyme from common wheat which converts tricetin sequentially to its tri-ether.
References
- ^ Enzyme 2.1.1.175 at KEGG Pathway Database.
- ^ Zhou JM, Fukushi Y, Wollenweber E, Ibrahim RK (2008). "Characterization of two O-methyltransferase-like genes in barley and maize". Pharm. Biol. 46: 26–34. doi:10.1080/13880200701729745.
- ^ Lee, Y.J.; Kim, B.G.; Chong, Y.; Lim, Y.; Ahn, J.H. (2008). "Cation dependent O-methyltransferases from rice". Planta. 227: 641–647. doi:10.1007/s00425-007-0646-4. PMID 17943312.
External links
- Tricin+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)