Difference between revisions of "Part:BBa K3496005"

Revision as of 14:37, 27 October 2020

Flavonoid 3'-hydroxylase

Flavonoid 3'-hydroxylase from Fragaria vesca Flavonoid 3′-hydroxylase is the last enzyme during the eriodictyol metabolic pathway which converts the substrate naringenin to the final product.

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Usage and Biology

Flavonoids are the class of plant secondary metabolites with C6-C3-C6 basic carbon skeleton famous for its high-value effects, such as, improving the body's anti-oxidation capacity and immunity.

The detailed skeletal structure flavonoids is a 2-phenylbenzopyranone where two phenyl groups (commonly named A- and B-ring) are banded with the C ring (three‑carbon bridge cyclized with oxygen) . According to the hydroxylation pattern of B-ring, flavonoids can be divided into three subclasses including B-ring 4’-hydroxylated, 3’,4’-dihydroxylated, and 3′,4’,5’-trihydroxylated flavonoids.

Eriodictyol, as a natural edible flavonoid, is mainly derived from lemon fruits. It has a hydroxyl group on the B ring and higher anti-oxidation activity. Both F3’H and F3’5’H can help format the 3’,4’-dihydroxylated Eriodictyol.

F3’H belongs to the Cytochrome P450 proteins (P450s), a huge group of heme-containing mixed oxidases catalyzing NADPH- or NADH-dependent oxygenation reactions. P450 exists in almost all cultures from microbes to Vertebrata. In life process, the P450 family is responsible for endogenous metabolism, the activity and degradation of exogenous compounds.

In the last step of eriodictyol metabolic pathway when P450 enzyme F3‘H hydroxylated naringenin to obtain the final product eriodictyol, it is supposed to happen in eukaryotic organisms instead of a prokaryotic cell which is unable to provide the membrane structure required for post-modification of the enzyme.

Resource

F3‘H is widely available from different plants, including Glycine max, Pilosella officinarum, Vitis vinifera, Plectranthus scutellarioides, Matthiola incana, Fragaria vesca. This part is derived from Fragaria vesca, with rather high enzymatic activity.

Sequence and Features