EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.3.2.12 | 2-oxepin-2(3H)-ylideneacetyl-CoA + H2O |
- |
Escherichia coli |
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde |
- |
? |
3.3.2.12 | 2-oxepin-2(3H)-ylideneacetyl-CoA + H2O |
addition of purified PaaZ enzyme to enzymatically produced epoxide and oxepin in the presence of PaaG protein leads to a complete NADP+-dependent conversion of epoxide and oxepin into 3-oxo-5,6-dehydrosuberyl-CoA. PaaZ functions as an oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase catalyzing the two-step conversion of the oxepin-CoA via the open-chain aldehyde intermediate to 3-oxo-5,6-dehydrosuberyl-CoA |
Escherichia coli |
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde |
- |
? |
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 | more |
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 |
Escherichia coli |
? |
- |
? |
3.3.2.12 | more |
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 | more |
bifunctional protein, catalyzing the reactions of 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase, EC 3.3.2.12, and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase, EC 1.17.1.7 |
Escherichia coli |
? |
- |
? |
3.3.2.12 | more |
enzyme additionally shows enoyl-CoA hydratase activity involved in supplying (R)-3-hydroxyacyl-CoA from the beta-oxidation pathway to polyhydroxyalkanoate biosynthetic pathway in the fadB mutant Escherichia coli strain |
Escherichia coli |
? |
- |
? |
3.3.2.12 | oxepin-CoA + H2O |
- |
Escherichia coli |
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde |
- |
? |
3.3.2.12 | oxepin-CoA + H2O |
100% activity |
Escherichia coli |
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde |
main product |
? |