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Chalcone synthase

Chalcone Synthase (Naringenin Chalcone Synthase)
Chalcone Synthase X Ray Image.png
The structure of CHS from Medicago sativa.
Identifiers
EC number 2.3.1.74
CAS number 56803-04-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Chalcone and stilbene synthases, C-terminal domain
Identifiers
Symbol Chal_sti_synt_C
Pfam PF02797
Pfam clan CL0046
InterPro IPR012328

Chalcone synthase or naringenin-chalcone synthase (CHS) is an enzyme ubiquitous to higher plants and belongs to a family of polyketide synthase enzymes (PKS) known as type III PKS. Type III PKSs are associated with the production of chalcones, a class of organic compounds found mainly in plants as natural defense mechanisms and as synthetic intermediates. CHS was the first type III PKS to be discovered. It is the first committed enzyme in flavonoid biosynthesis. The enzyme catalyzes the conversion of 4-coumaroyl-CoA and malonyl-CoA to naringenin chalcone.

CHS catalysis serves as the initial step for flavonoid biosynthesis. Flavonoids are important plant secondary metabolites that serve various functions in higher plants. These include pigmentation, UV protection, fertility, antifungal defense and the recruitment of nitrogen-fixing bacteria. CHS is believed to act as a central hub for the enzymes involved in the flavonoid pathway. Studies have shown that these enzymes interact via protein-protein interactions. Through FLIM FRET, it was shown that CHS interacts with chalcone isomerase (CHI), a consecutive step enzyme, as well as other non-consecutive step enzymes flavanone 3-hydroxylase (F3H), dihydroflavonol 4-reductase (DFR), and flavonol synthase I.

Naringenin-chalcone synthase uses malonyl-CoA and 4-coumaroyl-CoA to produce CoA, naringenin chalcone, and CO2.


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Wikipedia

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