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Literature summary for 4.1.1.9 extracted from
- Rat malonyl-CoA decarboxylase; cloning, expression in E. coli and its biochemical characterization (2002), J. Biochem. Mol. Biol., 35, 213-219.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| from brain, expression in Escherichia coli BL21, sequencing | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.068 | - |
malonyl-CoA | pH 7, recombinant MCD | Rattus norvegicus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | expression of recombinant MCD in a soluble and an insoluble form, the N-terminal 38 amino acids represents a putative mitochondrial targeting sequence, the last 3 amino acid sequences, SKL, represent peroxisomal targeting ones | Rattus norvegicus | - |
- |
| soluble | recombinant MCD, expression in a soluble and an insoluble form | Rattus norvegicus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
x * 54000, SDS-PAGE, x * 54610, full-length MCD, calculated from the amino acid sequence | Rattus norvegicus |
| 54610 | - |
x * 54000, SDS-PAGE, x * 54610, full-length MCD, calculated from the amino acid sequence | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Malonyl-CoA | Rattus norvegicus | may be implicated in the regulation of lipid metabolism and other cellular functions, involved in the regulation of the cellular malonyl-CoA level, may play an essential role in regulating energy utilization in response to various nutritional changes and/or pathological states | Acetyl-CoA + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | recombinant MCD has a different degree or lack of glycosylation from the original rat enzyme | Rattus norvegicus |
| proteolytic modification | the N-terminal 38 amino acids represents a putative mitochondrial targeting sequence, the last 3 amino acid sequences, SKL, represent peroxisomal targeting ones | Rattus norvegicus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant MCD | Rattus norvegicus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 43.4 | - |
pH 7, recombinant MCD | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Malonyl-CoA | high affinity for malonyl-CoA | Rattus norvegicus | Acetyl-CoA + CO2 | - |
? | |
| Malonyl-CoA | may be implicated in the regulation of lipid metabolism and other cellular functions, involved in the regulation of the cellular malonyl-CoA level, may play an essential role in regulating energy utilization in response to various nutritional changes and/or pathological states | Rattus norvegicus | Acetyl-CoA + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 54000, SDS-PAGE, x * 54610, full-length MCD, calculated from the amino acid sequence | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Rattus norvegicus |
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Release 2023.1 (January 2023)
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