Chalcone synthase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1d6h' size='340' side='right' caption=' | + | <StructureSection load='1d6h' size='340' side='right' caption='Alfalfa chalcone synthase containing sulfinoalanine complex with CoA and sulfate (PDB code [[1d6h]])' scene=''> |
==Function== | ==Function== | ||
| - | '''Chalcone synthase''' (CHS) is essential for the biosynthesis of flavonoids and anthocyanin pigments in plants. CHS condenses p-coumaroyl-CoA and three malonyl-CoA to produce naringenin | + | '''Chalcone synthase''' (CHS) is essential for the biosynthesis of flavonoids and anthocyanin pigments in plants. CHS condenses p-coumaroyl-CoA and three malonyl-CoA to produce the polyketide naringenin |
<ref>PMID:25404490</ref>. | <ref>PMID:25404490</ref>. | ||
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==Relevance== | ==Relevance== | ||
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| + | The CHS biosynthesis product naringenin has inhibitory activity on a Cyt P450 isoform which can have carcinogenic effect <ref>PMID:15744083</ref> and has significant antioxidant properties. | ||
== Structural highlights == | == Structural highlights == | ||
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| + | CHS active site residues (Cys-His-Asn) and Phe interact with coenzyme A. The Cys residue is the catalytic nucleophile tethering the starting group and the growing polyketide chain<ref>PMID:10653632</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:02, 1 February 2021
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Chalcone synthase
Updated on 01-February-2021
References
- ↑ Yu HN, Wang L, Sun B, Gao S, Cheng AX, Lou HX. Functional characterization of a chalcone synthase from the liverwort Plagiochasma appendiculatum. Plant Cell Rep. 2015 Feb;34(2):233-45. doi: 10.1007/s00299-014-1702-8. Epub 2014 , Nov 18. PMID:25404490 doi:http://dx.doi.org/10.1007/s00299-014-1702-8
- ↑ Kanno S, Tomizawa A, Hiura T, Osanai Y, Shouji A, Ujibe M, Ohtake T, Kimura K, Ishikawa M. Inhibitory effects of naringenin on tumor growth in human cancer cell lines and sarcoma S-180-implanted mice. Biol Pharm Bull. 2005 Mar;28(3):527-30. doi: 10.1248/bpb.28.527. PMID:15744083 doi:http://dx.doi.org/10.1248/bpb.28.527
- ↑ Jez JM, Ferrer JL, Bowman ME, Dixon RA, Noel JP. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry. 2000 Feb 8;39(5):890-902. PMID:10653632
