Trihydroxystilbene synthase
| Trihydroxystilbene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.95 | ||||||||
| CAS no. | 128449-70-7 | ||||||||
| 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 | ||||||||
| |||||||||
Trihydroxystilbene synthase (EC 2.3.1.95) is an enzyme that catalyzes the chemical reaction
The substrates of this enzyme characterised from peanut are one unit of coumaroyl-CoA and three units of malonyl-CoA. These combine to form one unit of resveratrol, with 4 units each of coenzyme A and carbon dioxide as byproducts.[1]
This enzyme belongs to the family of transferases, To be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing). Other names in common use include resveratrol synthase, and stilbene synthase.[2] This enzyme participates in phenylpropanoid biosynthesis.[3][4]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Z1E[5] and 1Z1F.[5]
References
- ^ Schöppner A, Kindl H (June 1984). "Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut" (PDF). The Journal of Biological Chemistry. 259 (11): 6806–11. doi:10.1016/S0021-9258(17)39799-5. PMID 6427224.
- ^ Enzyme 2.3.1.95 at KEGG Pathway Database.
- ^ Valletta, Alessio; Iozia, Lorenzo Maria; Leonelli, Francesca (January 2021). "Impact of Environmental Factors on Stilbene Biosynthesis". Plants. 10 (1): 90. Bibcode:2021Plnts..10...90V. doi:10.3390/plants10010090. PMC 7823792. PMID 33406721.
- ^ Dubrovina, A. S.; Kiselev, K. V. (October 2017). "Regulation of stilbene biosynthesis in plants". Planta. 246 (4): 597–623. Bibcode:2017Plant.246..597D. doi:10.1007/s00425-017-2730-8. ISSN 0032-0935. PMID 28685295. S2CID 4015467.
- ^ a b Shomura Y, Torayama I, Suh DY, Xiang T, Kita A, Sankawa U, Miki K (September 2005). "Crystal structure of stilbene synthase from Arachis hypogaea". Proteins. 60 (4): 803–6. doi:10.1002/prot.20584. PMID 16028220. S2CID 44490134.