Protein Domain : Chalcone/stilbene synthase, C-terminal IPR012328

Type  Domain
Description  Chalcone synthases (CHS) ( ) 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 catalyse 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) [ ]. 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 [, ].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 [ ].
Short Name  Chalcone/stilbene_synt_C

0 Child Features

0 Gene Families

1000 Genes

0 Ontology Annotations

0 Parent Features

13 Publications

USDA
InterMine logo
The Legume Information System (LIS) is a research project of the USDA-ARS:Corn Insects and Crop Genetics Research in Ames, IA.
LegumeMine || ArachisMine | CicerMine | GlycineMine | LensMine | LupinusMine | PhaseolusMine | VignaMine | MedicagoMine
InterMine © 2002 - 2022 Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, United Kingdom