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Literature summary for 4.2.1.17 extracted from

  • Binstock, J.F.; Schulz, H.
    Fatty acid oxidation complex from Escherichia coli (1981), Methods Enzymol., 71, 403-411 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
2-decenoyl-CoA
-
Escherichia coli
0.05
-
crotonyl-CoA
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
MW of multienzyme complex of fatty acid oxidation, EC 4.2.1.17/EC 1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3: 270000-300000 Da Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3 contains phospholipid Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-CoA + H2O the classification is ambiguous because the stereochemistry is not exactly determined Escherichia coli ?
-
?
decenoyl-CoA + H2O the classification is ambiguous because the stereochemistry is not exactly determined Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
crotonase multienzyme of fatty acid oxidation contains in addition to enoyl-CoA hydratase, EC 1.1.1.35 (L-3-hydroxyacyl-CoA dehydrogenase), EC 2.3.1.16 (3-ketoacyl-CoA thiolase), EC 5.1.2.2 (3-hydroxyacyl-CoA epimerase) and EC 5.3.3.3 (DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase) Escherichia coli