5.5.1.6: chalcone isomerase
This is an abbreviated version!
For detailed information about chalcone isomerase, go to the full flat file.
Word Map on EC 5.5.1.6
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5.5.1.6
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flavonoid
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anthocyanins
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dihydroflavonol
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ammonia-lyase
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naringenin
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phenylpropanoids
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anthocyanidin
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4-reductase
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cinnamate
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isoflavone
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flavone
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4-hydroxylase
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isoflavonoids
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3\'-hydroxylase
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3-o-glucosyltransferase
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r2r3-myb
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4-coumarate:coa
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leucoanthocyanidin
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4-coumarate
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3',5'-hydroxylase
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agriculture
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petroselinum
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2s-naringenin
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2s-flavanones
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analysis
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lindemuthianum
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4.3.1.5
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synthesis
- 5.5.1.6
- flavonoid
- anthocyanins
- dihydroflavonol
-
ammonia-lyase
- naringenin
-
phenylpropanoids
- anthocyanidin
-
4-reductase
- cinnamate
- isoflavone
- flavone
-
4-hydroxylase
-
isoflavonoids
-
3\'-hydroxylase
- 3-o-glucosyltransferase
-
r2r3-myb
-
4-coumarate:coa
-
leucoanthocyanidin
- 4-coumarate
-
3',5'-hydroxylase
- agriculture
- petroselinum
- 2s-naringenin
-
2s-flavanones
- analysis
- lindemuthianum
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4.3.1.5
- synthesis
Reaction
Synonyms
Chalcone isomerase, chalcone isomerase-like protein, Chalcone-flavanone isomerase, CHI, Chi-1, Chi1, CHI1A, CHI1B1, CHI1B2, CHI2, CHI2B1, CHI2B2, Chi3, CHI3A, CHI3A1, CHI3A2, CHI3B, CHI3B1, CHI3C1, CHI3C2, CHI4, CHI4A, CHI4B, CHIL, CHIL1, CHIL2, EFP, Isomerase, chalcone, MpCHI, SlCHI1, taxifolin-isomerizing enzyme, TRANSPARENT TESTA 5 protein, TT5, type IV CHI protein
ECTree
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KM Value
KM Value on EC 5.5.1.6 - chalcone isomerase
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additional information
additional information
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calculated and experimentally-derived free-energy barriers for the Michael addition of the deprotonated forms of chalcone and 6'-deoxychalcone in aqueous solution and enzyme. Substrates may exist in at least two different conformational forms according to the relative disposition of the carbonyl group and the alpha,beta-double bond. Only the S-trans conformer, which is not the most stable one in aqueous solution, is able to proceed up to the reaction products
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0.0053
mutant enzyme R34A, at pH 7.6 and 25°C
0.008
isoliquiritigenin
mutant enzyme I190M, at pH 7.6 and 25°C
0.0108
isoliquiritigenin
mutant enzyme S189T, at pH 7.6 and 25°C
0.0112
isoliquiritigenin
mutant enzyme K108A, at pH 7.6 and 25°C
0.0164
isoliquiritigenin
mutant enzyme M36A, at pH 7.6 and 25°C
0.0185
isoliquiritigenin
mutant enzyme S189A, at pH 7.6 and 25°C
0.0225
isoliquiritigenin
mutant enzyme Q104E, at pH 7.6 and 25°C
0.0243
isoliquiritigenin
mutant enzyme R34M, at pH 7.6 and 25°C
0.0276
isoliquiritigenin
mutant enzyme Y116A, at pH 7.6 and 25°C
0.0024
mutant enzyme S189A, at pH 7.6 and 25°C
0.0048
naringenin chalcone
mutant enzyme K108A, at pH 7.6 and 25°C
0.0048
naringenin chalcone
mutant enzyme M36A, at pH 7.6 and 25°C
0.0061
naringenin chalcone
mutant enzyme Q104E, at pH 7.6 and 25°C
0.007
naringenin chalcone
mutant enzyme Y116A, at pH 7.6 and 25°C
0.0085
naringenin chalcone
wild type enzyme, at pH 7.6 and 25°C
0.0086
naringenin chalcone
mutant enzyme I190M, at pH 7.6 and 25°C
0.0099
naringenin chalcone
mutant enzyme S189T, at pH 7.6 and 25°C
0.0105
naringenin chalcone
mutant enzyme M96K, at pH 7.6 and 25°C
0.0143
naringenin chalcone
mutant enzyme Y48F, at pH 6.4, temperature not specified in the publication
0.0203
naringenin chalcone
mutant enzyme H33A, at pH 6.4, temperature not specified in the publication
0.0439
naringenin chalcone
mutant enzyme H73A, at pH 6.4, temperature not specified in the publication
0.0567
naringenin chalcone
mutant enzyme R125A, at pH 6.4, temperature not specified in the publication
0.0798
naringenin chalcone
mutant enzyme H33Q, at pH 6.4, temperature not specified in the publication
0.1319
naringenin chalcone
mutant enzyme H33E, at pH 6.4, temperature not specified in the publication
0.354
naringenin chalcone
wild type enzyme, at pH 6.4, temperature not specified in the publication