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Literature summary for 2.3.1.74 extracted from

  • Shen, Y.; Li, X.; Chai, T.; Wang, H.
    Outer-sphere residues influence the catalytic activity of a chalcone synthase from Polygonum cuspidatum (2016), FEBS Open Bio, 6, 610-618 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.74

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-Rosetta (DE3) cells Polygonum cuspidatum

Protein Variants

Protein Variants Comment Organism
C198F the mutant almost completely loses the enzyme activity Polygonum cuspidatum
Q82P the mutant exhibits reduced chalcone-forming activity because its Km value with 4-coumaroyl-CoA as the starter substrate is about 2times higher than that of the wild type enzyme. Additionally, the mutant loses 4-hydroxybenzalacetone-forming activity at pH 7.0-9.0 Polygonum cuspidatum
Q82P/C198F the mutant exhibits benzalacetone synthase activity. The catalytic efficiencies of the mutant for 4-coumaroyl-CoA and malonyl-CoA are lower than that of wild type enzyme Polygonum cuspidatum
R105Q the mutant exhibits benzalacetone synthase activity. The catalytic efficiency of the mutant for 4-coumaroyl-CoA is higher than that of wild type enzyme Polygonum cuspidatum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0136
-
 4-coumaroyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0142
-
 4-coumaroyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0198
-
 4-coumaroyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0213
-
 4-coumaroyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0308
-
 malonyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0374
-
 malonyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0397
-
 malonyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.0579
-
 malonyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Polygonum cuspidatum H9DV62
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Polygonum cuspidatum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 malonyl-CoA + 4-coumaroyl-CoA
-
 Polygonum cuspidatum 4 CoA + naringenin chalcone + 3 CO2
-
 ?

Synonyms

Synonyms Comment Organism
Chs1
-
 Polygonum cuspidatum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.038
-
 malonyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.05
-
 4-coumaroyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.055
-
 malonyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.063
-
 malonyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.082
-
 malonyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.085
-
 4-coumaroyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.11
-
 4-coumaroyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
0.178
-
 4-coumaroyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Polygonum cuspidatum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.66
-
 malonyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
1.39
-
 malonyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
1.69
-
 malonyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
2.5
-
 4-coumaroyl-CoA mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
2.65
-
 malonyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
4.29
-
 4-coumaroyl-CoA mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
8.21
-
 4-coumaroyl-CoA wild type enzyme, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum
12.56
-
 4-coumaroyl-CoA mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication Polygonum cuspidatum