Naringenin-chalcone synthase

From Wikipedia, the free encyclopedia

In enzymology, a naringenin-chalcone synthase (EC 2.3.1.74) is an enzyme that catalyzes the chemical reaction

3 malonyl-CoA + 4-coumaroyl-CoA $\rightleftharpoons$ 4 CoA + naringenin chalcone + 3 CO₂

Thus, the two substrates of this enzyme are malonyl-CoA and 4-coumaroyl-CoA, whereas its 3 products are CoA, naringenin chalcone, and CO₂.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing). Other names in common use include chalcone synthase, flavanone synthase, 6'-deoxychalcone synthase, chalcone synthetase, DOCS, and CHS. This enzyme participates in flavonoid biosynthesis.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes 1BI5, 1BQ6, 1CGK, 1CGZ, 1CHW, 1CML, 1D6F, 1D6H, 1D6I, 1EE0, 1I86, 1I88, 1I89, 1I8B, 1JWX, 1QLV, 1TED, 1TEE, 1U0V, 1U0W, and 2P0U.

[edit] References

IUBMB entry for 2.3.1.74
BRENDA references for 2.3.1.74 (Recommended.)
PubMed references for 2.3.1.74
PubMed Central references for 2.3.1.74
Google Scholar references for 2.3.1.74
Ayabe S, Udagawa A, Furuya T (1988). "NAD(P)H-dependent 6'-deoxychalcone synthase activity in Glycyrrhiza echinata cells induced by yeast extract". Arch. Biochem. Biophys. 261: 458–62. doi:10.1016/0003-9861(88)90362-1. PMID 3355160.
Heller W, Hahlbrock K (1980). "Highly purified "flavanone synthase" from parsley catalyzes the formation of naringenin chalcone". Arch. Biochem. Biophys. 200: 617–9. doi:10.1016/0003-9861(80)90395-1. PMID 7436427.