|PROSITE documentation PDOC00403
Chalcone and stilbene synthases active site
Chalcone synthases (CHS) (EC 126.96.36.199) and stilbene synthases (STS) (formerly
known as resveratrol synthases) are related plant enzymes . CHS is an
important enzyme in flavanoid biosynthesis and STS 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
These enzymes are proteins of about 390 amino-acid residues. A conserved
cysteine residue, located in the central section of these proteins, has been
shown  to be essential for the catalytic activity of both enzymes and
probably represents the binding site for the 4-coumaryl-CoA group. The region
around this active site residue is well conserved and can be used as a
In addition to the plant enzymes, this family also includes Bacillus subtilis
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|CHALCONE_SYNTH, PS00441; Chalcone and stilbene synthases active site (PATTERN)
C is the active site residue
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1CGK 1CGZ 1U0U 1U0V ... [ALL]
||Schroeder J., Schroeder G.
||Z. Naturforsch. 45C:1-8(1990).
||Lanz T., Tropf S., Marner F.-J., Schroeder J., Schroeder G.
||The role of cysteines in polyketide synthases. Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways.
||J. Biol. Chem. 266:9971-9976(1991).
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