EzCatDB: D00453

DB codeD00453
CATH domainDomain 11.10.890.20
Domain 23.50.70.10Catalytic domain
E.C.5.5.1.6
CSA1eyp
MACiEM0196


Enzyme Name
Swiss-protKEGG

P28012
Protein nameChalcone--flavonone isomerase 1chalcone isomerase
chalcone-flavanone isomerase
SynonymsChalcone isomerase 1
EC 5.5.1.6

KEGG pathways
MAP codePathways
MAP00941Flavonoid biosynthesis

Swiss-prot:Accession NumberP28012
Entry nameCFI1_MEDSA
ActivityA chalcone = a flavanone.
Subunit
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC06561C09321C08650C00509C00766C09762
CompoundIsosalipurpol2'-HydroxychalconeIsoliquiritigeninNaringeninFlavanoneLiquiritigenin
Typearomatic ring (only carbon atom),carbohydratearomatic ring (only carbon atom),carbohydratearomatic ring (only carbon atom),carbohydratearomatic ring (only carbon atom),carbohydratearomatic ring (only carbon atom),carbohydratearomatic ring (only carbon atom),carbohydrate
1eypA01UnboundUnboundUnboundUnboundUnboundUnbound
1eypB01UnboundUnboundUnboundUnboundUnboundUnbound
1eyqA01UnboundUnboundUnboundUnboundUnboundUnbound
1eyqB01UnboundUnboundUnboundUnboundUnboundUnbound
1fm7A01UnboundUnboundUnboundUnboundUnboundUnbound
1fm7B01UnboundUnboundUnboundUnboundUnboundUnbound
1fm8A01UnboundUnboundUnboundUnboundUnboundUnbound
1fm8B01UnboundUnboundUnboundUnboundUnboundUnbound
1jepA01UnboundUnboundUnboundUnboundUnboundUnbound
1jepB01UnboundUnboundUnboundUnboundUnboundUnbound
1jx0A01UnboundUnboundUnboundUnboundUnboundUnbound
1jx0B01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1A01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1B01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1C01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1D01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1E01UnboundUnboundUnboundUnboundUnboundUnbound
1jx1F01UnboundUnboundUnboundUnboundUnboundUnbound
1eypA02UnboundUnboundUnboundUnboundUnboundUnbound
1eypB02UnboundUnboundUnboundUnboundUnboundUnbound
1eyqA02UnboundUnboundUnboundBound:NARUnboundUnbound
1eyqB02UnboundUnboundUnboundBound:NARUnboundUnbound
1fm7A02UnboundUnboundUnboundUnboundUnboundBound:DFV
1fm7B02UnboundUnboundUnboundUnboundUnboundBound:DFV
1fm8A02UnboundUnboundUnboundUnboundAnalogue:DDCUnbound
1fm8B02UnboundUnboundUnboundUnboundAnalogue:DDCUnbound
1jepA02UnboundUnboundUnboundUnboundAnalogue:DFLUnbound
1jepB02UnboundUnboundUnboundUnboundAnalogue:DFLUnbound
1jx0A02UnboundUnboundUnboundUnboundUnboundBound:DFV
1jx0B02UnboundUnboundUnboundUnboundUnboundUnbound
1jx1A02UnboundUnboundUnboundUnboundUnboundUnbound
1jx1B02UnboundUnboundUnboundUnboundUnboundUnbound
1jx1C02UnboundUnboundUnboundUnboundUnboundBound:DFV
1jx1D02UnboundUnboundUnboundUnboundUnboundUnbound
1jx1E02UnboundUnboundUnboundUnboundUnboundUnbound
1jx1F02UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [6], [8] & [13]
pdbCatalytic residuescomment
1eypA01

1eypB01

1eyqA01

1eyqB01

1fm7A01

1fm7B01

1fm8A01

1fm8B01

1jepA01

1jepB01

1jx0A01

1jx0B01

1jx1A01

1jx1B01

1jx1C01

1jx1D01

1jx1E01

1jx1F01

1eypA02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1eypB02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1eyqA02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1eyqB02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1fm7A02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1fm7B02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1fm8A02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1fm8B02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1jepA02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1jepB02THR 48;LYS 97;TYR 106;LYS 109;ASN 113;THR 190

1jx0A02THR 48;LYS 97;       ;LYS 109;ASN 113;THR 190
mutant Y106F
1jx0B02THR 48;LYS 97;       ;LYS 109;ASN 113;THR 190
mutant Y106F
1jx1A02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A
1jx1B02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A
1jx1C02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A
1jx1D02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A
1jx1E02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A
1jx1F02      ;LYS 97;TYR 106;LYS 109;ASN 113;THR 190
mutant T48A

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]SCHEME 2, p.396-3981
[6]Fig.4, p.788-7892
[8]Fig.5, p.5175-51762
[9]Fig.1, p.1367-13692
[11]Chart 1A
[13]Scheme 1, p.27332

references
[1]
PubMed ID2760066
JournalJ Biol Chem
Year1989
Volume264
Pages14272-6
AuthorsBednar RA, Fried WB, Lock YW, Pramanik B
TitleChemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site.
[2]
PubMed ID2241159
JournalArch Biochem Biophys
Year1990
Volume282
Pages393-8
AuthorsBednar RA, Adeniran AJ
TitleChemical modification of chalcone isomerase by diethyl pyrocarbonate: histidine residues are not essential for catalysis.
[3]
PubMed ID2340265
JournalBiochemistry
Year1990
Volume29
Pages3684-90
AuthorsBednar RA
TitleReactivity and pH dependence of thiol conjugation to N-ethylmaleimide: detection of a conformational change in chalcone isomerase.
[4]
PubMed ID1772902
JournalBioconjug Chem
Year1991
Volume2
Pages211-6
AuthorsBednar RA, McCaffrey C, Shan K
TitleIntroduction of unnatural amino acids into chalcone isomerase.
[5]
PubMed ID11024274
JournalGene
Year2000
Volume255
Pages127-38
AuthorsSaslowsky DE, Dana CD, Winkel-Shirley B
TitleAn allelic series for the chalcone synthase locus in Arabidopsis.
[6]
CommentsX-ray crystallography
PubMed ID10966651
JournalNat Struct Biol
Year2000
Volume7
Pages786-91
AuthorsJez JM, Bowman ME, Dixon RA, Noel JP
TitleStructure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase.
Related PDB1eyp,1eyq
[7]
PubMed ID11553733
JournalPlant Physiol
Year2001
Volume127
Pages46-57
AuthorsDong X, Braun EL, Grotewold E
TitleFunctional conservation of plant secondary metabolic enzymes revealed by complementation of Arabidopsis flavonoid mutants with maize genes.
[8]
CommentsX-ray crystallography
PubMed ID11955065
JournalBiochemistry
Year2002
Volume41
Pages5168-76
AuthorsJez JM, Bowman ME, Noel JP
TitleRole of hydrogen bonds in the reaction mechanism of chalcone isomerase.
Related PDB1jx0,1jx1
[9]
CommentsX-ray crystallography
PubMed ID11698411
JournalJ Biol Chem
Year2002
Volume277
Pages1361-9
AuthorsJez JM, Noel JP
TitleReaction mechanism of chalcone isomerase. pH dependence, diffusion control, and product binding differences.
Related PDB1fm7,1fm8,1jep
[10]
PubMed ID12527208
JournalGene
Year2003
Volume302
Pages171-8
AuthorsDruka A, Kudrna D, Rostoks N, Brueggeman R, von Wettstein D, Kleinhofs A
TitleChalcone isomerase gene from rice (Oryza sativa) and barley (Hordeum vulgare): physical, genetic and mutation mapping.
[11]
PubMed ID12568595
JournalJ Am Chem Soc
Year2003
Volume125
Pages1472-3
AuthorsHur S, Bruice TC
TitleEnzymes do what is expected (chalcone isomerase versus chorismate mutase).
[12]
PubMed ID12644647
JournalPlant Physiol
Year2003
Volume131
Pages941-51
AuthorsShimada N, Aoki T, Sato S, Nakamura Y, Tabata S, Ayabe S
TitleA cluster of genes encodes the two types of chalcone isomerase involved in the biosynthesis of general flavonoids and legume-specific 5-deoxy(iso)flavonoids in Lotus japonicus.
[13]
PubMed ID14978275
JournalProc Natl Acad Sci U S A
Year2004
Volume101
Pages2730-5
AuthorsHur S, Newby ZE, Bruice TC
TitleTransition state stabilization by general acid catalysis, water expulsion, and enzyme reorganization in Medicago savita chalcone isomerase.

comments
This enzyme catalyzes intramolecular condensation.

createdupdated
2004-07-302009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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