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Literature summary for 2.3.1.196 extracted from
- The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate (2005), Plant J., 44, 606-619.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Vitis labrusca |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | - |
Vitis labrusca |  |
| Zn2+ | - |
Vitis labrusca | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00842 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme | Vitis labrusca | |
| 0.0118 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme | Vitis labrusca | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM | Vitis labrusca | |
| K+ | the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM | Vitis labrusca | |
| Mg2+ | the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM | Vitis labrusca | |
| Mn2+ | the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM | Vitis labrusca | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
x * 50000, SDS-PAGE | Vitis labrusca |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vitis labrusca | Q3ZPN4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Vitis labrusca |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| berry | the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp | Vitis labrusca | - |
| mesocarp | the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp | Vitis labrusca | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzoyl-CoA + benzyl alcohol | - |
Vitis labrusca | CoA + benzyl benzoate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 50000, SDS-PAGE | Vitis labrusca |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 22 | assay at | Vitis labrusca |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
30 min, stable | Vitis labrusca |
| 45 | - |
5 min, 80% loss of activity | Vitis labrusca |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.045 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme | Vitis labrusca | |
| 0.045 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme | Vitis labrusca | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Vitis labrusca |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9 | stable | Vitis labrusca |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.85 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme | Vitis labrusca | |
| 3.81 | - |
benzoyl-CoA | pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme | Vitis labrusca | |
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Release 2023.1 (January 2023)
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