3.3.2.12: oxepin-CoA hydrolase
This is an abbreviated version!
For detailed information about oxepin-CoA hydrolase, go to the full flat file.
Reaction
Synonyms
EC 3.7.1.16, ECH-Aa, MaoC, oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+), paaZ, PaaZ-ECH
ECTree
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Substrates Products
Substrates Products on EC 3.3.2.12 - oxepin-CoA hydrolase
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REACTION DIAGRAM
crotonyl-CoA + H2O
(R)-3-hydroxybutyryl-CoA
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the enzyme shows 1% activity with crotonyl-CoA compared to oxepin-CoA
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3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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2-oxepin-2(3H)-ylideneacetyl-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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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
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oxepin-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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100% activity
main product
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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