Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.3.8 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
Search for more literature for 5.3.3.8

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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
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

Organism

Organism UniProt Comment Textmining
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

Posttranslational Modification Comment Organism
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

Subunits

Subunits Comment Organism
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