Chalcone/stilbene synthase, C-terminal (IPR012328)

Short name: Chalcone/stilbene_synth_C

Overlapping homologous superfamilies


Domain relationships



Chalcone synthases (CHS) (EC: and stilbene synthases (STS) (formerly known as resveratrol synthases) are related plant enzymes. CHS is an important enzyme in flavanoid biosynthesis and STS is a key enzyme in stilbene-type phyloalexin biosynthesis. Both enzymes catalyze the addition of three molecules of malonyl-CoA to a starter CoA ester (a typical example is 4-coumaroyl-CoA), producing either a chalcone (with CHS) or stilbene (with STS) [PMID: 2184816].

These enzymes have a conserved cysteine residue, located in the central section of the protein sequence, which is essential for the catalytic activity of both enzymes and probably represents the binding site for the 4-coumaryl-CoA group [PMID: 2033084].

This domain of chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in the N-terminal domain [PMID: 10426957].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.