Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli DH5alpha cells | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
E256Q | inactive | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.056 | - |
NADP+ | pH and temperature not specified in the publication | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
amylose resin column chromatography, gel filtration | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O | - |
Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+ | - |
? | |
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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional fusion proteom | Escherichia coli |
paaZ | - |
Escherichia coli |
PaaZ-ALDH | domain showing 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase activity | Escherichia coli |
PacL | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Escherichia coli |