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Literature summary extracted from

  • Stoops, J.K.; Wakil, S.J.
    Animal fatty acid synthetase. A novel arrangement of the beta-ketoacyl synthetase sites comprising domains of the two subunits (1981), J. Biol. Chem., 256, 5128-5133.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.85 1,3-Dibromo-2-propanone acetyl-CoA, not malonyl-CoA, protects against inactivation, both protect against cross-linking of the subunits; covalently cross-links subunits, inactivates beta-ketoacyl synthetase- and overall-fatty acid synthase reaction Gallus gallus
2.3.1.85 iodoacetamide inhibits beta-ketoacyl synthetase activity, acetyl-CoA but not malonyl CoA protects Gallus gallus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.85 220000
-
 2 * 220000, SDS-PAGE Gallus gallus
2.3.1.85 480000
-
 SDS-PAGE Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.85 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.85
-
 Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.85 liver
-
 Gallus gallus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.85 1.2
-
 NADPH Gallus gallus

Subunits

EC Number Subunits Comment Organism
2.3.1.85 dimer 2 * 220000, SDS-PAGE Gallus gallus
2.3.1.85 More condensing enzyme activity requires both subunits Gallus gallus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.85 25
-
 assay at Gallus gallus