EC Number | Cloned (Comment) | Organism |
---|---|---|
6.2.1.12 | overexpression in Escherichia coli | Acetobacterium woodii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.12 | 0.013 | - |
ATP | 30°C, pH 7.0 | Acetobacterium woodii | |
6.2.1.12 | 0.025 | - |
caffeate | 30°C, pH 7.0 | Acetobacterium woodii | |
6.2.1.12 | 0.5 | - |
CoA | 30°C, pH 7.0 | Acetobacterium woodii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.8.3.23 | soluble | - |
Acetobacterium woodii | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.12 | K+ | strictly K+-dependent. Half-maximal activity is obtained at 6 mM K+ | Acetobacterium woodii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.8.3.23 | 57700 | - |
x * 57700, calculated | Acetobacterium woodii |
6.2.1.12 | 60000 | - |
x * 60000, SDS-PAGE | Acetobacterium woodii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.12 | ATP + caffeate + CoA | Acetobacterium woodii | the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion | AMP + diphosphate + caffeoyl-CoA | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.3.23 | Acetobacterium woodii | F1CYZ5 | - |
- |
6.2.1.12 | Acetobacterium woodii | F1CYZ6 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.2.1.12 | - |
Acetobacterium woodii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.12 | ATP + 4-coumarate + CoA | 52% of the activity with caffeate | Acetobacterium woodii | AMP + diphosphate + 4-coumaroyl-CoA | - |
? | |
6.2.1.12 | ATP + caffeate + CoA | - |
Acetobacterium woodii | AMP + diphosphate + caffeoyl-CoA | - |
? | |
6.2.1.12 | ATP + caffeate + CoA | the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion | Acetobacterium woodii | AMP + diphosphate + caffeoyl-CoA | - |
? | |
6.2.1.12 | ATP + cinnamate + CoA | 9% of the activity with caffeate | Acetobacterium woodii | AMP + diphosphate + cinnamoyl-CoA | - |
? | |
6.2.1.12 | ATP + ferulate + CoA | 16% of the activity with caffeate | Acetobacterium woodii | AMP + diphosphate + feruloyl-CoA | - |
? | |
6.2.1.12 | additional information | no activity with either sinapate or 4-hydroxybenzoate. The more hydroxyl groups are present, the better is the activity of the enzyme. Methoxy groups on the aromatic ring have a negative effect on enzyme activity. It is possible that methoxy groups cause a steric obstruction. No activity can be measured if there is no acryl group present in the substrate | Acetobacterium woodii | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.8.3.23 | ? | x * 57700, calculated | Acetobacterium woodii |
6.2.1.12 | ? | x * 60000, SDS-PAGE | Acetobacterium woodii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.8.3.23 | CarA | - |
Acetobacterium woodii |
2.8.3.23 | YdiF | - |
Acetobacterium woodii |
6.2.1.12 | caffeoyl-CoA ligase | - |
Acetobacterium woodii |
6.2.1.12 | caffeoyl-CoA synthetase | - |
Acetobacterium woodii |
6.2.1.12 | caffeoyl-coenzyme A synthetase | - |
Acetobacterium woodii |
6.2.1.12 | CarB | - |
Acetobacterium woodii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.2.1.12 | 25 | 40 | - |
Acetobacterium woodii |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.12 | 5.5 | - |
CoA | 30°C, pH 7.0 | Acetobacterium woodii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.2.1.12 | 6 | 8 | - |
Acetobacterium woodii |
EC Number | Organism | Comment | Expression |
---|---|---|---|
2.8.3.23 | Acetobacterium woodii | there is no induction by p-hydroxybenzoate or syringate | additional information |
2.8.3.23 | Acetobacterium woodii | expression of the car operon is induced by caffeate, p-coumarate, ferulate, and cinnamate and also by sinapate | up |
6.2.1.12 | Acetobacterium woodii | CarE and CarD (and thus the caffeate reduction operon) are induced in cells grown in the presence of cinnamate, sinapate, caffeate, ferulate, or 4-coumarate | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.8.3.23 | physiological function | coenzyme A transferase CarA, acyl-CoA synthetase CarB, and acyl-CoA dehydrogenase CarC are part of the caffeate respiration pathway | Acetobacterium woodii |
6.2.1.12 | metabolism | the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion | Acetobacterium woodii |