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