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Literature summary extracted from

  • Leanz, G.F.; Hammes, G.G.
    Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase (1986), Biochemistry, 25, 5617-5624.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.39 pyridoxal 5'-phosphate 4 mM at 30°C for 15 min on complete fatty acid synthase selectively and completely inactivates Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.39 additional information
-
 additional information NADP+ binds to enzyme in anti conformation both between nicotinamide-ribose and adenine-ribose Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.39 additional information Gallus gallus part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.39 Gallus gallus
-
 chicken
-

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.39 crotonyl-N-acetyl-cysteamine + NADPH
-
 Gallus gallus butyryl-N-acetyl-cysteamine + NADP+
-
 ?
1.3.1.39 additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Gallus gallus ?
-
 ?

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.3.1.39 7.2
-
 activity of entire fatty acid synthase declined no more than 15% in 24 h at pH 7.2 in phosphate puffer Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.39 NADPH
-
 Gallus gallus