Chalcone isomerase

Enzyme responsible for some flavanones From Wikipedia, the free encyclopedia

Chalcone isomerase (EC 5.5.1.6) is an enzyme that catalyzes the general chemical reaction

a chalcone a flavanone
Quick facts Identifiers, Symbol ...
Chalcone isomerase
chalcone isomerase complexed with 4'-hydroxyflavanone
Identifiers
SymbolChalcone
PfamPF02431
InterProIPR003466
SCOP21eyp / SCOPe / SUPFAM
Available protein structures:
PDB  IPR003466 PF02431 (ECOD; PDBsum)  
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In the biosynthesis of anthocyanins in plants, an important example of this reaction converts the chalcone produced by chalcone synthase to naringenin:[1][2]

This reaction can occur spontaneously but provides racemic material. The enzyme constrains the reaction to give only the (S) isomer of the flavanone.[1][3]

This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is flavanone lyase (decyclizing). This enzyme is also called chalcone-flavanone isomerase. This enzyme participates in flavonoid biosynthesis.

The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ChiB, but only the first seems to encode a functional chalcone isomerase.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1EYP, 1EYQ, 1FM7, 1FM8, 1JEP, 1JX0, and 1JX1.

Chalcone isomerase has a core 2-layer alpha/beta structure consisting of beta(3)-alpha(2)-beta-alpha(2)-beta(3).[4]

References

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