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Literature summary for 3.3.2.12 extracted from

  • Teufel, R.; Gantert, C.; Voss, M.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
    Studies on the mechanism of ring hydrolysis in phenylacetate degradation: A metabolic branching point (2011), J. Biol. Chem., 286, 11021-11034.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli DH5alpha cells Escherichia coli

KM Value [mM]

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose resin column chromatography Escherichia coli

Substrates and Products (Substrate)

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

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 [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Escherichia coli