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

BRENDA support

Literature summary for 2.3.1.85 extracted from

  • Wu, B.N.; Park, Y.D.; Tian, W.X.; Zhou, H.M.
    Unfolding and inactivation of fatty acid synthase from chicken liver during urea denaturation (2001), Biochim. Biophys. Acta, 1549, 112-121.
    View publication on PubMed
Search for more literature for 2.3.1.85

Inhibitors

Inhibitors Comment Organism Structure
Urea non-competitive inhibitor for NADPH, competitive inhibitor for acetyl-CoA and malonyl-CoA, complete inactivation occurs at lower concentration than obvious conformational changes, aggregation occurs at 3-4 M Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+
-
 Gallus gallus palmitate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Gallus gallus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
210
-
 Urea substrate NADPH Gallus gallus
570
-
 Urea substrate malonyl-CoA Gallus gallus
580
-
 Urea substrate acetyl-CoA Gallus gallus