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Literature summary for 2.3.1.85 extracted from

  • Carlisle-Moore, L.; Gordon, C.R.; Machutta, C.A.; Miller, W.T.; Tonge, P.J.
    Substrate recognition by the human fatty-acid synthase (2005), J. Biol. Chem., 280, 42612-42618.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.85

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes are expressed in Sf9 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
K1699A specific activity is 10% of wild-type value Homo sapiens
K1699Q specific activity is 7.5% of wild-type value Homo sapiens
S2151A inactive enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
 acetyl-CoA 25°C, pH 7.0, mutant enzyme K1699Q Homo sapiens
0.001
-
 malonyl-CoA 25°C, pH 7.0, mutant enzyme K1699Q Homo sapiens
0.003
-
 malonyl-CoA 25°C, pH 7.0, mutant enzyme K1699A Homo sapiens
0.005
-
 NADPH 25°C, pH 7.0, wild-type enzyme Homo sapiens
0.006
-
 malonyl-CoA 25°C, pH 7.0, wild-type enzyme Homo sapiens
0.007
-
 acetyl-CoA 25°C, pH 7.0, wild-type enzyme Homo sapiens
0.007
-
 acetyl-CoA 25°C, pH 7.0, mutant enzyme K1699A Homo sapiens
0.37
-
 NADPH 25°C, pH 7.0, mutant enzyme K1699A Homo sapiens
0.4
-
 NADPH 25°C, pH 7.0, mutant enzyme K1699Q Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
 acetyl-CoA mutant enzyme K1699Q Homo sapiens
0.3
-
 malonyl-CoA mutant enzyme K1699Q Homo sapiens
0.32
-
 acetyl-CoA mutant enzyme K1699A Homo sapiens
0.32
-
 malonyl-CoA mutant enzyme K1699A Homo sapiens
2.7
-
 acetyl-CoA wild-type enzyme Homo sapiens
2.7
-
 malonyl-CoA wild-type enzyme Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Homo sapiens