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Trihydroxystilbene synthase

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(Redirected from Resveratrol synthase)
trihydroxystilbene synthase
Identifiers
EC no.2.3.1.95
CAS no.128449-70-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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.[1] This enzyme participates in phenylpropanoid biosynthesis.[1][2]

Structural studies

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As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Z1E[3] and 1Z1F.[3]

References

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  1. ^ a b Valletta, Alessio; Iozia, Lorenzo Maria; Leonelli, Francesca (January 2021). "Impact of Environmental Factors on Stilbene Biosynthesis". Plants. 10 (1): 90. doi:10.3390/plants10010090. PMC 7823792. PMID 33406721.
  2. ^ Dubrovina, A. S.; Kiselev, K. V. (October 2017). "Regulation of stilbene biosynthesis in plants". Planta. 246 (4): 597–623. doi:10.1007/s00425-017-2730-8. ISSN 0032-0935. PMID 28685295. S2CID 4015467.
  3. ^ 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.

Further reading

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