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Literature summary for 1.3.8.1 extracted from

  • Beinert, H.
    Acyl Coenzyme A dehydrogenase (1963), The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. ), 7, 447-466.
No PubMed abstract available
Search for more literature for 1.3.8.1

Inhibitors

Inhibitors Comment Organism Structure
2-butenoyl-CoA competitive product inhibition Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 butyryl-CoA electron transfer protein as acceptor Sus scrofa
0.02
-
 butyryl-CoA phenazine methyl sulfate as acceptor Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Sus scrofa 5739
-

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyryl-CoA + electron acceptor
-
 Sus scrofa 2-butenoyl-CoA + reduced acceptor
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.5
-
 butyryl-CoA electron transfer protein as acceptor Sus scrofa
9.17
-
 butyryl-CoA phenazine methyl sulfate as acceptor Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8 6.9 with electron transfer flavoprotein Sus scrofa
7.6
-
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol per mol of subunit Sus scrofa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00036
-
 2-butenoyl-CoA
-
 Sus scrofa