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Literature summary for 1.3.8.7 extracted from

  • Wu, J.; Bell, A.F.; Luo, L.; Stephens, A.W.; Stankovich, M.T.; Tonge, P.J.
    Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy (2003), Biochemistry, 42, 11846-11856.
    View publication on PubMed
Search for more literature for 1.3.8.7

Protein Variants

Protein Variants Comment Organism
E276Q no detectable activity in ferricenium assay Sus scrofa
E376P no detectable activity in ferricenium assay Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0022
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD Sus scrofa
0.0023
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, native enzyme Sus scrofa
0.0025
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, recombinant wild-type enzyme Sus scrofa
0.0026
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
octanoyl-CoA + ferricenium
-
 Sus scrofa 2-octenoyl-CoA + reduced acceptor
-
 ?

Synonyms

Synonyms Comment Organism
medium-chain acyl-CoA dehydrogenase
-
 Sus scrofa
pMCAD
-
 Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.047
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD Sus scrofa
18.8
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, recombinant wild-type enzyme Sus scrofa
19.6
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, native enzyme Sus scrofa
20
-
 octanoyl-CoA 25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Sus scrofa