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Literature summary for 1.3.8.7 extracted from

  • Gopalan, K.V.; Srivastava, D.K.
    Beyond the proton abstracting role of Glu-376 in medium-chain acyl-CoA dehydrogenase: influence of Glu-376-->Gln substitution on ligand binding and catalysis (2002), Biochemistry, 41, 4638-4648.
    View publication on PubMed
Search for more literature for 1.3.8.7

Protein Variants

Protein Variants Comment Organism
E376Q mutation slows down the octanoyl-CoA-dependent reductive half-reaction of the enzyme by about 5 orders of magnitude due to impairment in the proton transfer step, also impairs the association and dissociation rates for the binding of the reaction product octenoyl-CoA. Km-value for octanoyl-CoA is 1.6fold reduced, turnover number for octenoyl-CoA is 7083fold reduced compared to wild-type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0021
-
 octanoyl-CoA pH 7.6, 25°C, mutant enzyme E376Q Homo sapiens
0.003
-
 octanoyl-CoA pH 7.6, 25°C, wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
octanoyl-CoA + ferriocenium hexfluorophosphate
-
 Homo sapiens 2-octenoyl-CoA + reduced acceptor
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0024
-
 octanoyl-CoA pH 7.6, 25°C, mutant enzyme E376Q Homo sapiens
17
-
 octanoyl-CoA pH 7.6, 25°C, wild-type enzyme Homo sapiens