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Literature summary extracted from
- Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase (2004), Protein Expr. Purif., 37, 434-442.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.5.8.4 | overexpression in Escherichia coli strain JM109 as N-terminally His-tagged enzyme being equally distributed in the soluble fraction and the insoluble inclusion body fraction | Rattus norvegicus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.8.4 | 0.05 | - |
N,N-dimethylglycine | pH 7.0, 30°C, recombinant holoenzyme, 2 Km-values | Rattus norvegicus |  |
| 1.5.8.4 | 9.4 | - |
N,N-dimethylglycine | pH 7.0, 30°C, recombinant holoenzyme, 2 Km-values | Rattus norvegicus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.5.8.4 | mitochondrion | - |
Rattus norvegicus | 5739 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.8.4 | 90000 | - |
x * 90000, native enzyme, SDS-PAGE, x * 93000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
| 1.5.8.4 | 93000 | - |
x * 90000, native enzyme, SDS-PAGE, x * 93000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.8.4 | 5,10-methenyltetrahydrofolate + FADH2 | Rattus norvegicus | - |
5,10-methylene tetrahydrofolate + FAD | - |
? | |
| 1.5.8.4 | N,N-dimethylglycine + H2O + FAD | Rattus norvegicus | - |
sarcosine + formaldehyde + FADH2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.8.4 | Rattus norvegicus | - |
male Wistar rats | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.8.4 | native enzyme from liver mitochondria, recombinant His-tagged enzyme from Escherichia coli 45fold by nickel affinity chromatography | Rattus norvegicus |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.5.8.4 | refolding by 80fold dilution after solubilization from inclusion bodies by urea treatment, 50-60% reactivation yield, overview | Rattus norvegicus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.5.8.4 | liver | - |
Rattus norvegicus | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.5.8.4 | 0.24 | - |
purified recombinant enzyme from soluble fraction | Rattus norvegicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.8.4 | 5,10-methenyltetrahydrofolate + FADH2 | - |
Rattus norvegicus | 5,10-methylene tetrahydrofolate + FAD | - |
? | |
| 1.5.8.4 | N,N-dimethylglycine + H2O + FAD | - |
Rattus norvegicus | sarcosine + formaldehyde + FADH2 | - |
? | |
| 1.5.8.4 | N,N-dimethylglycine + H2O + oxidized 1-methoxy-5-methylphenazinium methylsulfate | - |
Rattus norvegicus | sarcosine + formaldehyde + reduced 1-methoxy-5-methylphenazinium methylsulfate | - |
? | |
| 1.5.8.4 | N,N-dimethylglycine + H2O + oxidized 2,6-dichlorophenolindophenol | - |
Rattus norvegicus | sarcosine + formaldehyde + reduced 2,6-dichlorophenolindophenol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.5.8.4 | ? | x * 90000, native enzyme, SDS-PAGE, x * 93000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.8.4 | Me2GlyDH | - |
Rattus norvegicus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.5.8.4 | 45 | - |
recombinant and native enzyme | Rattus norvegicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.5.8.4 | 8.5 | - |
recombinant and native enzyme | Rattus norvegicus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.8.4 | FAD | absolutely required, covalently bound to the apoenzyme via a histidinyl(N3)-(8alpha)FAD linkage, cofactor-free apoenzyme shows 70% reduced activity compared to the holoenzyme | Rattus norvegicus | |
| 1.5.8.4 | additional information | 1-methoxy-5-methylphenazinium methylsulfate can act as electron acceptor | Rattus norvegicus | |
| 1.5.8.4 | additional information | 2,6-dichlorophenolindophenol can act as electron acceptor | Rattus norvegicus |
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