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Literature summary for 1.3.1.39 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
Search for more literature for 1.3.1.39

Inhibitors

Inhibitors Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
 chicken
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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

Cofactor Comment Organism Structure
NADPH
-
 Gallus gallus