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Literature summary for 1.1.1.100 extracted from

  • Venkatesan, R.; Sah-Teli, S.K.; Awoniyi, L.O.; Jiang, G.; Prus, P.; Kastaniotis, A.J.; Hiltunen, J.K.; Wierenga, R.K.; Chen, Z.
    Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase (2014), Nat. Commun., 5, 4805.
    View publication on PubMed
Search for more literature for 1.1.1.100

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (RARE) cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 15-18% (w/v) PEG3350 and 0.4 M ammonium acetate in sodium acetate buffer at pH 5.0 Homo sapiens

Protein Variants

Protein Variants Comment Organism
D42A the mutant shows 36% activity with acetoacetyl-CoA and NADH, 20% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 26% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
K152A the mutant shows 109% activity with acetoacetyl-CoA and NADH, no activity with acetoacetyl-CoA and NADPH, 123% activity with 9,10-phenanthrene and NAD+, and 2.2% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
K169E the mutant shows 95% activity with acetoacetyl-CoA and NADH, 5.5% activity with acetoacetyl-CoA and NADPH, 76% activity with 9,10-phenanthrene and NAD+, and 6% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
K173A the mutant shows 0.3% activity with acetoacetyl-CoA and NADH, 2.4% activity with acetoacetyl-CoA and NADPH, 6% activity with 9,10-phenanthrene and NAD+, and 22% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
Q126E/K169E the mutant shows 156% activity with acetoacetyl-CoA and NADH, 4.3% activity with acetoacetyl-CoA and NADPH, 84% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
Q126E/R168E/K169E the mutant shows 72% activity with acetoacetyl-CoA and NADH, 0.5% activity with acetoacetyl-CoA and NADPH, 40% activity with 9,10-phenanthrene and NAD+, and no activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
R168E the mutant shows 106% activity with acetoacetyl-CoA and NADH, 6.3% activity with acetoacetyl-CoA and NADPH, 38% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
R34A the mutant shows 102% activity with acetoacetyl-CoA and NADH, 100% activity with acetoacetyl-CoA and NADPH, 40.44% activity with 9,10-phenanthrene and NAD+, and 2.1% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens
Y169A the mutant shows 3% activity with acetoacetyl-CoA and NADH, 2% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 15% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92506 cf EC 1.1.1.62
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex 200 gel filtration Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.06
-
 mutant enzyme K173A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
0.44
-
 mutant enzyme R34A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
0.44
-
 mutant enzyme R34A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
0.46
-
 mutant enzyme K152A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
0.5
-
 mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
0.65
-
 mutant enzyme Y169A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
0.85
-
 mutant enzyme Y169A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
1.2
-
 mutant enzyme K173A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
1.3
-
 mutant enzyme K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
1.6
-
 mutant enzyme R168E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
1.7
-
 mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
2
-
 mutant enzyme Y169A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
2.4
-
 mutant enzyme K173A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
2.6
-
 wild type enzyme, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
3.1
-
 mutant enzyme Y169A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
3.5
-
 wild type enzyme, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
4.3
-
 mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
4.5
-
 mutant enzyme K173A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
5.4
-
 mutant enzyme D42A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C Homo sapiens
5.5
-
 mutant enzyme K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
6.3
-
 mutant enzyme R168E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
7.3
-
 mutant enzyme D42A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
7.9
-
 mutant enzyme R168E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
8.4
-
 mutant enzyme Q126E/R168E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
14.8
-
 mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
15.7
-
 mutant enzyme K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
17.4
-
 mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
19.3
-
 mutant enzyme K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
20
-
 mutant enzyme D42A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C Homo sapiens
20.5
-
 wild type enzyme, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
20.7
-
 mutant enzyme R34A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
20.8
-
 wild type enzyme, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
21
-
 mutant enzyme R34A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
21.7
-
 mutant enzyme R168E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
22
-
 mutant enzyme K152A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
25.5
-
 mutant enzyme K152A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens
31.8
-
 mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C Homo sapiens
74.6
-
 mutant enzyme D42A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
9,10-phenanthrene quinone + NADH + H+
-
 Homo sapiens ?
-
 ?
9,10-phenanthrene quinone + NADPH + H+ low activity with NADPH Homo sapiens ?
-
 ?
acetoacetyl-CoA + NADH + H+
-
 Homo sapiens ?
-
 ?
acetoacetyl-CoA + NADPH + H+ low activity with NADPH Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
heterotetramer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase
-
 Homo sapiens
3-ketoacyl-thioester reductase
-
 Homo sapiens
KAR
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Homo sapiens
NADPH low activity with NADPH Homo sapiens