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Literature summary for 1.3.8.7 extracted from
- Characterization of wild-type human medium-chain acyl-CoA dehydrogenase (MCAD) and mutant enzymes present in MCAD-deficient patients by two-dimensional gel electrophoresis: evidence for post-translational modification of the enzyme (1994), Biochem. Med. Metab. Biol., 52, 36-44.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| heterologous expression of wild-type, K304E and R28C mutant enzymes from patients with medium chain acyl-CoA dehydrogenase deficiency, in Escherichia coli and COS-7 cells | 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 | - |
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Release 2023.1 (January 2023)
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