Cloned (Comment) | Organism |
---|---|
expression of wild-type and G553M mutant enzymes in an enzyme-deficient Saccharomyces cerevisiae strain | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
G553M | site-directed mutagenesis, the mutant enzyme shows altered substrate specificity: highly reduced activity with medium- and long-chain acyl-CoAs and increased activity with acetyl-CoA and butanoyl-CoA compared to the wild-type enzyme | Rattus norvegicus |
additional information | the carnitine acetyl-transferase, specific for acetyl-CoA/short-chain acyl-CoAs, can be modified to an enzyme with elevated carnitine octanoyltransferase activity by mutation of Met564 to Gly, overview | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Rattus norvegicus | 5739 | - |
peroxisome | - |
Rattus norvegicus | 5777 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
69000 | - |
x * 69000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
octanoyl-CoA + L-carnitine | Rattus norvegicus | - |
CoA + L-octanoylcarnitine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine | acyl-CoA substrate specificity is determined by Gly553, active site structure and substrate positioning modeling | Rattus norvegicus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
acyl-CoA substrate specificity of wild-type and G553M mutant enzymes, overview | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-carnitine | low activity | Rattus norvegicus | CoA + L-acetylcarnitine | - |
? | |
butanoyl-CoA + L-carnitine | - |
Rattus norvegicus | CoA + L-butanoylcarnitine | - |
? | |
decanoyl-CoA + L-carnitine | best substrate | Rattus norvegicus | CoA + L-decanoylcarnitine | - |
? | |
dodecanoyl-CoA + L-carnitine | - |
Rattus norvegicus | CoA + L-dodecanoylcarnitine | - |
? | |
hexadecanoyl-CoA + L-carnitine | low activity | Rattus norvegicus | CoA + L-hexadecanoylcarnitine | - |
? | |
hexanoyl-CoA + L-carnitine | best substrate | Rattus norvegicus | CoA + L-hexanoylcarnitine | - |
? | |
additional information | acyl-CoA substrate specificity is determined by Gly553 | Rattus norvegicus | ? | - |
? | |
octanoyl-CoA + L-carnitine | - |
Rattus norvegicus | CoA + L-octanoylcarnitine | - |
? | |
tetradecanoyl-CoA + L-carnitine | - |
Rattus norvegicus | CoA + L-tetradecanoylcarnitine | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 69000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
More | active site structure and substrate positioning modeling for wild-type and G553M mutant enzymes | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
carnitine octanoyltransferase | - |
Rattus norvegicus |
COT | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Rattus norvegicus |