Biology:Trihydroxystilbene synthase

From HandWiki
Short description: Class of enzymes
Trihydroxystilbene synthase
Identifiers
EC number2.3.1.95
CAS number128449-70-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

  1. REDIRECT Template: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

  1. "Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut". The Journal of Biological Chemistry 259 (11): 6806–11. June 1984. doi:10.1016/S0021-9258(17)39799-5. PMID 6427224. http://www.jbc.org/content/259/11/6806.full.pdf. 
  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" (in en). Plants 10 (1): 90. doi:10.3390/plants10010090. PMID 33406721. Bibcode2021Plnts..10...90V. 
  4. Dubrovina, A. S.; Kiselev, K. V. (October 2017). "Regulation of stilbene biosynthesis in plants" (in en). Planta 246 (4): 597–623. doi:10.1007/s00425-017-2730-8. ISSN 0032-0935. PMID 28685295. Bibcode2017Plant.246..597D. http://link.springer.com/10.1007/s00425-017-2730-8. 
  5. 5.0 5.1 "Crystal structure of stilbene synthase from Arachis hypogaea". Proteins 60 (4): 803–6. September 2005. doi:10.1002/prot.20584. PMID 16028220.