Naringenin-chalcone synthase
| naringenin-chalcone synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
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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
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, to be specific 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.
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.
References
- 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 (2): 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 (2): 617–9. doi:10.1016/0003-9861(80)90395-1. PMID 7436427.