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Literature summary for 1.2.1.91 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
Search for more literature for 1.2.1.91

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
E256Q inactive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.056
-
 NADP+ 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, gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O
-
 Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
-
 ?
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 ?
-
 ?

Synonyms

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Escherichia coli