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Literature summary extracted from

  • Kieweg, V.; Krautle, F.G.; Nandy, A.; Engst, S.; Vock, P.; Abdel-Ghany, A.G.; Bross, P.; Gregersen, N.; Rasched, I.; Strauss, A.; Ghisla, S.
    Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme (1997), Eur. J. Biochem., 246, 548-556.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.7 expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli Homo sapiens
1.3.8.7 expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.7 0.002
-
 hexadecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.0033
-
 dodecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.0035
-
 octanoyl-CoA
-
 Sus scrofa
1.3.8.7 0.0052
-
 tetradecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.0075
-
 hexanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.0077
-
 decanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.009
-
 hexanoyl-CoA
-
 Sus scrofa
1.3.8.7 0.012
-
 octanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 0.09
-
 butanoyl-CoA
-
 Sus scrofa
1.3.8.7 0.12
-
 butanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.7 Homo sapiens
-
 K304E point mutation leading to a higher susceptibility of the mutant enzyme for degradation is one of several mutations, which are responsible for medium chain acyl-CoA dehydrogenase deficiency
-
1.3.8.7 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.7 recombinant wild-type and K304E mutant enzyme Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.8.7 17.5
-
 recombinant K304E mutant enzyme, measured with ferricenium assay Homo sapiens
1.3.8.7 24.9
-
 recombinant wild-type enzyme, measured with ferricenium assay Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.7 butanoyl-CoA + acceptor
-
 Homo sapiens crotonyl-CoA + reduced acceptor
-
 ?
1.3.8.7 butanoyl-CoA + acceptor
-
 Sus scrofa crotonyl-CoA + reduced acceptor
-
 ?
1.3.8.7 hexanoyl-CoA + ferricenium
-
 Sus scrofa trans-hex-2-enoyl-CoA + ferrocenium
-
 r

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.8.7
-
 37 biphasic inactivation, half-lives: 3 h, fast phase, and more than 700 h, slow phase, at 28°C and 2 h, fast phase, and approx. 230 h, slow phase, at 37°C for the wild-type enzyme, the corresponding values for the K304E mutant enzyme are 1.7 h, 100 h at 28°C and 1.25 h and 55 h at 37°C Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.8.7 0.667
-
 octadecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 2.92
-
 hexadecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 6.33
-
 butanoyl-CoA ferricenium assay Sus scrofa
1.3.8.7 8.33
-
 tetradecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 8.83
-
 decanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 9
-
 butanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 9.5
-
 dodecanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 12.7
-
 hexanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 16.2
-
 octanoyl-CoA K304E mutant enzyme, ferricenium assay Homo sapiens
1.3.8.7 18.3
-
 octanoyl-CoA ferricenium assay Sus scrofa
1.3.8.7 20.8
-
 hexanoyl-CoA ferricenium assay Sus scrofa