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Literature summary 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)

EC Number Cloned (Comment) Organism
1.2.1.91 expressed in Escherichia coli DH5alpha cells Escherichia coli
3.3.2.12 expressed in Escherichia coli DH5alpha cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.91 E256Q inactive Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.91 0.056
-
 NADP+ pH and temperature not specified in the publication Escherichia coli
3.3.2.12 0.011
-
 oxepin-CoA pH and temperature not specified in the publication Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.91 Escherichia coli
-
-
-
3.3.2.12 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.91 amylose resin column chromatography, gel filtration Escherichia coli
3.3.2.12 amylose resin column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.91 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O
-
 Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
-
 ?
1.2.1.91 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 ?
-
 ?
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 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 ?
-
 ?
3.3.2.12 oxepin-CoA + H2O 100% activity Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde main product ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.91 oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) bifunctional fusion proteom Escherichia coli
1.2.1.91 paaZ
-
 Escherichia coli
1.2.1.91 PaaZ-ALDH domain showing 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase activity Escherichia coli
1.2.1.91 PacL
-
 Escherichia coli
3.3.2.12 ECH-Aa
-
 Escherichia coli
3.3.2.12 oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) bifunctional fusion proteom Escherichia coli
3.3.2.12 paaZ
-
 Escherichia coli
3.3.2.12 PaaZ-ECH domain showing oxepin-CoA hydrolase activity Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.3.2.12 39
-
 oxepin-CoA pH and temperature not specified in the publication Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.91 8
-
-
 Escherichia coli
3.3.2.12 8
-
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.91 NADP+
-
 Escherichia coli