Phloroisovalerophenone synthase
From Wikipedia, the free encyclopedia
In enzymology, a phloroisovalerophenone synthase (EC 2.3.1.156) is an enzyme that catalyzes the chemical reaction
- isovaleryl-CoA + 3 malonyl-CoA
4 CoASH + 3 CO2 + 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
Thus, the two substrates of this enzyme are isovaleryl-CoA and malonyl-CoA, whereas its 3 products are CoASH, CO2, and 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is isovaleryl-CoA:malonyl-CoA acyltransferase. Other names in common use include valerophenone synthase, and 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase.
[edit] References
- IUBMB entry for 2.3.1.156
- BRENDA references for 2.3.1.156 (Recommended.)
- PubMed references for 2.3.1.156
- PubMed Central references for 2.3.1.156
- Google Scholar references for 2.3.1.156
- Verpoorte R (1997). "Enzymes from the biosynthesis of hop alpha and beta acids". Proc. 26th Congr. Eur. Brew. Conv.: 215–221.
- G, Verpoorte R and Schroder J (1998). "4-Hydroxy-2-pyrone formation by chalcone and stilbene synthase with nonphysiological substrates". Phytochemistry 49: 1945–1951. doi:.

