EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.91 | expressed in Escherichia coli DH5alpha cells | Escherichia coli |
3.3.2.12 | expressed in Escherichia coli DH5alpha cells | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.91 | E256Q | inactive | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.91 | 0.056 | - |
NADP+ | pH and temperature not specified in the publication | Escherichia coli | |
3.3.2.12 | 0.011 | - |
oxepin-CoA | pH and temperature not specified in the publication | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.91 | Escherichia coli | - |
- |
- |
3.3.2.12 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.91 | amylose resin column chromatography, gel filtration | Escherichia coli |
3.3.2.12 | amylose resin column chromatography | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.91 | 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O | - |
Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+ | - |
? | |
1.2.1.91 | additional information | the bifunctional protein also use oxepin-CoA as substrate yielding 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde as main product and shows 1% activity with crotonyl-CoA compared to oxepin-CoA | Escherichia coli | ? | - |
? | |
3.3.2.12 | crotonyl-CoA + H2O | the enzyme shows 1% activity with crotonyl-CoA compared to oxepin-CoA | Escherichia coli | (R)-3-hydroxybutyryl-CoA | - |
? | |
3.3.2.12 | additional information | the bifunctional protein also use 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and NADP+ as substrate yielding 3-oxo-5,6-dehydrosuberyl-CoA as main product. The PaaZ-ECH domain acts as (R)-specific hydratase and shows no activity with (S)-3-hydroxybutyryl-CoA | Escherichia coli | ? | - |
? | |
3.3.2.12 | oxepin-CoA + H2O | 100% activity | Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde | main product | ? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.91 | oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional fusion proteom | Escherichia coli |
1.2.1.91 | paaZ | - |
Escherichia coli |
1.2.1.91 | PaaZ-ALDH | domain showing 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase activity | Escherichia coli |
1.2.1.91 | PacL | - |
Escherichia coli |
3.3.2.12 | ECH-Aa | - |
Escherichia coli |
3.3.2.12 | oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional fusion proteom | Escherichia coli |
3.3.2.12 | paaZ | - |
Escherichia coli |
3.3.2.12 | PaaZ-ECH | domain showing oxepin-CoA hydrolase activity | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.3.2.12 | 39 | - |
oxepin-CoA | pH and temperature not specified in the publication | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.91 | 8 | - |
- |
Escherichia coli |
3.3.2.12 | 8 | - |
- |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.91 | NADP+ | - |
Escherichia coli |