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Literature summary extracted from

  • Hall, C.L.
    Acyl-CoA dehydrogenases and electron-transferring flavoprotein (1978), Methods Enzymol., 53, 502-518.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.7 0.001
-
 octanoyl-CoA
-
 Sus scrofa
1.3.8.7 0.01
-
 electron transferring flavoprotein
-
 Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.8.7 42000
-
 4 * 42000, SDS-PAGE Sus scrofa
1.3.8.7 155000
-
 enzyme from heart, SDS-PAGE after cross-linkage with dimethylsuberimidate Bos taurus
1.3.8.7 160000
-
 SDS-PAGE after cross-linkage with dimethylsuberimidate Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.7 Bos taurus
-
-
-
1.3.8.7 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.7
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.7 liver
-
 Sus scrofa
-
1.3.8.7 liver
-
 Bos taurus
-

Storage Stability

EC Number Storage Stability Organism
1.3.8.7 -70°C, concentrated form, more than 1 year, no loss of activity Sus scrofa
1.3.8.7 -70°C, concentrated form, more than 1 year, no loss of activity Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.7 octanoyl-CoA + electron transferring flavoprotein
-
 Sus scrofa 2-octenoyl-CoA + reduced electron transferring flavoprotein
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.7 tetramer
-
 Bos taurus
1.3.8.7 tetramer 4 * 42000, SDS-PAGE Sus scrofa