1. References

In enzymology, a flavonol synthase ({{EC number|1.14.11.23}}) is an enzyme that catalyzes the following chemical reaction :

dihydroflavonol + 2-oxoglutarate + {{chem|O|2}} a flavonol + succinate + C{{chem|O|2}} + H₂O

The 3 substrates of this enzyme are dihydroflavonol, 2-oxoglutarate, and O₂, whereas its 4 products are flavonol, succinate, CO₂, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with {{chem|O|2}} as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from {{chem|O|2}} with 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. The systematic name of this enzyme class is dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in flavonoid biosynthesis.

References

• {{cite journal | vauthors = Wellmann F, Lukacin R, Moriguchi T, Britsch L, Schiltz E, Matern U | date = 2002 | title = Functional expression and mutational analysis of flavonol synthase from Citrus unshiu | journal = Eur. J. Biochem. | volume = 269 | pages = 4134–42 | pmid = 12180990 | doi = 10.1046/j.1432-1033.2002.03108.x | issue = 16 }}
• {{cite journal | vauthors = Lukacin R, Wellmann F, Britsch L, Martens S, Matern U | date = 2003 | title = Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase | journal = Phytochemistry | volume = 62 | pages = 287–92 | pmid = 12620339 | doi = 10.1016/S0031-9422(02)00567-8 | issue = 3 }}
• {{cite journal | vauthors = Martens S, Forkmann G, Britsch L, Wellmann F, Matern U, Lukacin R | date = 2003 | title = Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley | journal = FEBS Lett. | volume = 544 | pages = 93–8 | pmid = 12782296 | doi = 10.1016/S0014-5793(03)00479-4 | issue = 1-3 }}
• {{cite journal | author = CJ | date = 2004 | title = Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3beta-hydroxylase | journal = J. Biol. Chem. | volume = 279 | pages = 1206–16 | pmid = 14570878 | doi = 10.1074/jbc.M309228200 | last2 = Nakajima | first2 = J | last3 = Welford | first3 = RW | last4 = Yamazaki | first4 = M | last5 = Saito | first5 = K | last6 = Schofield | first6 = CJ | issue = 2 }}

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