Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Vitis labrusca |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Vitis labrusca | |
Zn2+ | - |
Vitis labrusca |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00251 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme | Vitis labrusca | |
0.00478 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme | Vitis labrusca | |
0.015 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme | Vitis labrusca | |
0.032 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme | Vitis labrusca |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
x * 50000, SDS-PAGE | Vitis labrusca |
50200 | - |
x * 50200, calculated from sequence | Vitis labrusca |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
anthraniloyl-CoA + methanol | Vitis labrusca | the enzyme is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the Washington Concord grape (Vitis labrusca) | CoA + O-methyl anthranilate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vitis labrusca | Q3ZPN4 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Vitis labrusca |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
anthraniloyl-CoA + methanol | the enzyme is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the Washington Concord grape (Vitis labrusca) | Vitis labrusca | CoA + O-methyl anthranilate | - |
? | |
anthraniloyl-CoA + methanol | the enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. The enzyme also shows benzyl alcohol O-benzoyltransferase activity, EC 2.3.1.196 | Vitis labrusca | CoA + O-methyl anthranilate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 50000, SDS-PAGE | Vitis labrusca |
? | x * 50200, calculated from sequence | Vitis labrusca |
Synonyms | Comment | Organism |
---|---|---|
AMAT | - |
Vitis labrusca |
anthraniloyl-coenzyme A (CoA):methanol acyltransferase | - |
Vitis labrusca |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 22 | assay at | Vitis labrusca |
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 Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0035 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme | Vitis labrusca | |
0.0058 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme | Vitis labrusca | |
0.01 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme | Vitis labrusca | |
0.022 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme | Vitis labrusca |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Vitis labrusca |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
7 | 9 | stable | Vitis labrusca |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme | Vitis labrusca | |
0.24 | - |
methanol | pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme | Vitis labrusca | |
2.07 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme | Vitis labrusca | |
8.9 | - |
anthraniloyl-CoA | pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme | Vitis labrusca |