Phenylpropanoids metabolism


The biosynthesis of phenylpropanoids involves a number of enzymes.

From amino acids to cinnamates

In plants, all phenylpropanoids are derived from the amino acids phenylalanine and tyrosine.
Phenylalanine ammonia-lyase is an enzyme that transforms L-phenylalanine and tyrosine into trans-cinnamic acid and p-coumaric acid, respectively.
Trans-cinnamate 4-monooxygenase is the enzyme that transforms trans-cinnamate into 4-hydroxycinnamate. 4-Coumarate-CoA ligase is the enzyme that transforms 4-coumarate into 4-coumaroyl-CoA.

Enzymes associated with biosynthesis of hydroxycinnamic acids

These enzymes conjugate phenylpropanoids to other molecules.
An alternative bacterial ketosynthase-directed stilbenoids biosynthesis pathway exists in Photorhabdus bacterial symbionts of Heterorhabditis nematodes, producing 3,5-dihydroxy-4-isopropyl-trans-stilbene for antibiotic purposes.

[Coumarin]s biosynthesis

can be combined with malonyl-CoA to yield the true backbone of flavonoids, a group of compounds called chalconoids, which contain two phenyl rings. Naringenin-chalcone synthase is an enzyme that catalyzes the following conversion:

Flavonoids biosynthesis

Conjugate ring-closure of chalcones results in the familiar form of flavonoids, the three-ringed structure of a flavone.

Biodegradation

Hydroxycinnamic acids degradation