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Literature summary for 2.3.1.16 extracted from

  • Pawar, S.; Schulz, H.
    The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli (1981), J. Biol. Chem., 256, 3894-3899.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
2 * 78000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit, SDS-PAGE Escherichia coli
78000
-
2 * 78000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit, SDS-PAGE Escherichia coli
260000
-
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit of the tetramer, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA + 3-oxoacyl-CoA
-
Escherichia coli acyl-CoA + acetyl-CoA
-
?
CoA + 3-oxoacyl-CoA
-
Escherichia coli B / ATCC 11303 acyl-CoA + acetyl-CoA
-
?

Subunits

Subunits Comment Organism
tetramer 2 * 78000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit, SDS-PAGE Escherichia coli