Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli DH5alpha cells | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.011 | - |
oxepin-CoA | pH and temperature not specified in the publication | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
amylose resin column chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
crotonyl-CoA + H2O | the enzyme shows 1% activity with crotonyl-CoA compared to oxepin-CoA | Escherichia coli | (R)-3-hydroxybutyryl-CoA | - |
? | |
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 | ? | - |
? | |
oxepin-CoA + H2O | 100% activity | Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde | main product | ? |
Synonyms | Comment | Organism |
---|---|---|
ECH-Aa | - |
Escherichia coli |
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional fusion proteom | Escherichia coli |
paaZ | - |
Escherichia coli |
PaaZ-ECH | domain showing oxepin-CoA hydrolase activity | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
39 | - |
oxepin-CoA | pH and temperature not specified in the publication | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Escherichia coli |