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Literature summary for 1.3.8.7 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
Search for more literature for 1.3.8.7

Cloned(Commentary)

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
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
-
Sus scrofa
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
 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]

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