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Literature summary for 1.3.8.7 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-
liver
-
Bos taurus
-

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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