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Trihydroxystilbene synthase

From Wikipedia, the free encyclopedia
Trihydroxystilbene synthase
Identifiers
EC no.2.3.1.95
CAS no.128449-70-7
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Trihydroxystilbene synthase (EC 2.3.1.95) is an enzyme that catalyzes the chemical reaction

+ 3
 
 
 
4 CO2
Rightward reaction arrow with minor product(s) to top right
 
 
 
 

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

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As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes PDB: 1Z1E[5] and PDB: 1Z1F.[5]

References

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  1. 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.
  2. Enzyme 2.3.1.95 at KEGG Pathway Database.
  3. 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.
  4. 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.
  5. 1 2 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.