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Literature summary extracted from

  • Gloerich, J.; Ruiter, J.P.; van den Brink, D.M.; Ofman, R.; Ferdinandusse, S.; Wanders, R.J.
    Peroxisomal trans-2-enoyl-CoA reductase is involved in phytol degradation (2006), FEBS Lett., 580, 2092-2096.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.3.1.38 stable for at least a month, when stored at -20°C in PBS containing 50% (v/v) glycerol Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.38 0.018
-
 trans-phytenoyl-CoA 37°C, pH 7.2 Homo sapiens
1.3.1.38 0.106
-
 NADPH 37°C, pH 7.2 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.38 peroxisome
-
 Homo sapiens 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.38 75000
-
 x * 75000, calculated and SDs-PAGE of enzyme fused to maltose-binding protein Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.38 Homo sapiens
-
 expression in Escherichia coli fused to maltose-binding protein
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.38 nervonyl-CoA + NADPH
-
 Homo sapiens tetracosanoyl-CoA + NADP+ 1% of the activity with trans-phytenoyl-CoA ir
1.3.1.38 octa-2-enoyl-CoA + NADPH
-
 Homo sapiens octanoyl-CoA + NADP+
-
 ir
1.3.1.38 trans-phytenoyl-CoA + NADPH + H+
-
 Homo sapiens phytanoyl-CoA + NADP+
-
 ir

Subunits

EC Number Subunits Comment Organism
1.3.1.38 ? x * 75000, calculated and SDs-PAGE of enzyme fused to maltose-binding protein Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.3.1.38 TER
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.38 7 7.5
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.38 NADP+
-
 Homo sapiens