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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.3.1.16 N-ethylmaleimide
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.35 42000
-
 2 * 78000 + 2 * 42000, SDS-PAGE Escherichia coli
1.1.1.35 78000
-
 2 * 78000 + 2 * 42000, SDS-PAGE Escherichia coli
1.1.1.35 260000
-
 gel filtration Escherichia coli
2.3.1.16 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
2.3.1.16 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
2.3.1.16 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
4.2.1.17 78000
-
 x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE Escherichia coli
4.2.1.17 160000
-
 multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC 1.1.1.35/EC2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, gel filtration, non-denaturing PAGE Escherichia coli
4.2.1.17 420000
-
 x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE Escherichia coli
5.1.2.3 additional information
-
 multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, MW 260000, native PAGE, gel filtration Escherichia coli
5.1.2.3 42000
-
 multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE Escherichia coli
5.1.2.3 78000
-
 multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE Escherichia coli
5.3.3.8 42000
-
 2 * 42000 + 2 * 78000, multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, SDS-PAGE Escherichia coli
5.3.3.8 78000
-
 2 * 42000 + 2 * 78000, multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, SDS-PAGE Escherichia coli
5.3.3.8 260000
-
 multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+ Escherichia coli
-
 acetoacetyl-CoA + NADH
-
 r
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+ Escherichia coli B / ATCC 11303
-
 acetoacetyl-CoA + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.35 Escherichia coli
-
-
-
2.3.1.16 Escherichia coli
-
-
-
4.2.1.17 Escherichia coli
-
-
-
4.2.1.17 Escherichia coli B / ATCC 11303
-
-
-
5.1.2.3 Escherichia coli
-
 B
-
5.1.2.3 Escherichia coli B / ATCC 11303
-
 B
-
5.3.3.8 Escherichia coli
-
 multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.2.1.17 lipoprotein 63 nmol of lipid phosphate per mg of protein, phosphatidylethanolamine, phosphatidylglycerol, cardiolipin. 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
5.1.2.3 lipoprotein the multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, contains 63 nmol of lipid phosphate per mg of protein Escherichia coli
5.3.3.8 lipoprotein multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, contains 63 nmol of lipid per mg of protein: phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.16 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
4.2.1.17
-
 Escherichia coli
5.1.2.3 multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3 Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.16 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
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.35 20
-
-
 Escherichia coli
2.3.1.16 additional information
-
-
 Escherichia coli
5.1.2.3 additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+
-
 Escherichia coli acetoacetyl-CoA + NADH
-
 r
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+
-
 Escherichia coli B / ATCC 11303 acetoacetyl-CoA + NADH
-
 r
2.3.1.16 CoA + 3-oxoacyl-CoA
-
 Escherichia coli acyl-CoA + acetyl-CoA
-
 ?
2.3.1.16 CoA + 3-oxoacyl-CoA
-
 Escherichia coli B / ATCC 11303 acyl-CoA + acetyl-CoA
-
 ?
4.2.1.17 crotonyl-CoA + H2O the classification is ambiguous because the stereochemistry is not exactly determined Escherichia coli ?
-
 ?
4.2.1.17 crotonyl-CoA + H2O the classification is ambiguous because the stereochemistry is not exactly determined Escherichia coli B / ATCC 11303 ?
-
 ?
5.1.2.3 D-3-Hydroxydodecanoyl-CoA
-
 Escherichia coli L-3-Hydroxydodecanoyl-CoA
-
 ?
5.1.2.3 D-3-Hydroxydodecanoyl-CoA
-
 Escherichia coli B / ATCC 11303 L-3-Hydroxydodecanoyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.35 tetramer 2 * 78000 + 2 * 42000, SDS-PAGE Escherichia coli
2.3.1.16 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
4.2.1.17 ? x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE Escherichia coli
5.1.2.3 More multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE Escherichia coli
5.3.3.8 tetramer 2 * 42000 + 2 * 78000, multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, SDS-PAGE Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.35 NAD+
-
 Escherichia coli