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Literature summary for 2.3.1.74 extracted from
- Outer-sphere residues influence the catalytic activity of a chalcone synthase from Polygonum cuspidatum (2016), FEBS Open Bio, 6, 610-618 .
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 | |
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