Trihydroxystilbene synthase
| trihydroxystilbene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.95 | ||||||||
| CAS number | 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 / EGO | ||||||||
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In enzymology, a trihydroxystilbene synthase (EC 2.3.1.95) is an enzyme that catalyzes the chemical reaction
- 3 malonyl-CoA + 4-coumaroyl-CoA 4 CoA + 3,4',5-trihydroxy-stilbene + 4 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and 4-coumaroyl-CoA, whereas its 3 products are CoA, 3,4',5-trihydroxy-stilbene (resveratrol), and CO2.
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. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Z1E[1] and 1Z1F.[1]
References
- 1 2 Shomura, Yasuhito; Torayama, Ichiro; Suh, Dae-Yeon; Xiang, Ting; Kita, Akiko; Sankawa, Ushio; Miki, Kunio (2005). "Crystal structure of stilbene synthase from Arachis hypogaea". Proteins: Structure, Function, and Bioinformatics. 60 (4): 803–806. doi:10.1002/prot.20584.
- Schöppner, Anne; Kindl, Helmut (1984). "Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut" (PDF). J. Biol. Chem. 259 (11): 6806–6811. PMID 6427224.