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Literature summary for 2.3.1.74 extracted from

  • Waki, T.; Imaizumi, R.; Uno, K.; Doi, Y.; Tsunashima, M.; Yamada, S.; Mameda, R.; Nakata, S.; Yanai, T.; Takeshita, K.; Sakai, N.; Kataoka, K.; Yamamoto, M.; Takahashi, S.; Nakayama, T.; Yamashita, S.
    Structural insights into catalytic promiscuity of chalcone synthase from Glycine max (L.) Merr. Coenzyme A-induced alteration of product specificity (2024), Biochem. Biophys. Res. Commun., 718, 150080.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Glycine max

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme bound to CoA and naringenin Glycine max

Protein Variants

Protein Variants Comment Organism
K268A the mutation results in an enhanced naringenin chalcone/4-coumaroyltriacetic acid lactone production ratio. The catalytic efficiency of the mutant is 54% of that observed in the wild type enzyme Glycine max
K55A the mutant exhibits greater catalytic efficiency for total tetraketide production compared to the wild type, with increase of 4.1fold Glycine max
R68A the mutant exhibits greater catalytic efficiency for total tetraketide production compared to the wild type, with increase of 2.5fold Glycine max

Inhibitors

Inhibitors Comment Organism Structure
CoA in the presence of at least 1 mM CoA, the enzyme almost exclusively produces CTAL and amost no THC Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00333
-
 4-coumaroyl-CoA mutant enzyme K55A, pH and temperature not specified in the publication Glycine max
0.00771
-
 4-coumaroyl-CoA wild type enzyme, pH and temperature not specified in the publication Glycine max
0.012
-
 4-coumaroyl-CoA mutant enzyme K268A, pH and temperature not specified in the publication Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3 malonyl-CoA + 4-coumaroyl-CoA Glycine max
-
 4 CoA + naringenin chalcone + 3 CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Glycine max P24826
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Glycine max

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 malonyl-CoA + 4-coumaroyl-CoA
-
 Glycine max 4 CoA + naringenin chalcone + 3 CO2
-
 ?
additional information under the assay conditions, the enzyme exclusively catalyzes the production of naringenin chalcone and CTAL3 from 3 malonyl-CoA and 4-coumaroyl-CoA. In the presence of at least 1 mM CoA, the enzyme almost exclusively produces CTAL Glycine max ?
-
-

Subunits

Subunits Comment Organism
homodimer
-
 Glycine max

Synonyms

Synonyms Comment Organism
Chs1
-
 Glycine max

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0517
-
 4-coumaroyl-CoA mutant enzyme K268A, pH and temperature not specified in the publication Glycine max
0.0617
-
 4-coumaroyl-CoA wild type enzyme, pH and temperature not specified in the publication Glycine max
0.109
-
 4-coumaroyl-CoA mutant enzyme K55A, pH and temperature not specified in the publication Glycine max

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.067
-
 wild type enzyme, pH and temperature not specified in the publication Glycine max CoA

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3
-
 4-coumaroyl-CoA mutant enzyme K268A, pH and temperature not specified in the publication Glycine max
8
-
 4-coumaroyl-CoA wild type enzyme, pH and temperature not specified in the publication Glycine max
20
-
 4-coumaroyl-CoA mutant enzyme R58A, pH and temperature not specified in the publication Glycine max
33
-
 4-coumaroyl-CoA mutant enzyme K55A, pH and temperature not specified in the publication Glycine max