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Literature summary for 2.1.3.1 extracted from
- New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii (2007), Prep. Biochem. Biotechnol., 37, 13-26.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 5S subunit of enzyme | Propionibacterium freudenreichii subsp. shermanii |
| the gene encoding the 5S subunit is cloned into the pTXB1 vector | Propionibacterium freudenreichii subsp. shermanii |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 55500 | - |
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit | Propionibacterium freudenreichii subsp. shermanii |
| 55620 | - |
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit | Propionibacterium freudenreichii subsp. shermanii |
| 55623 | - |
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit | Propionibacterium freudenreichii subsp. shermanii |
| 55700 | - |
5S subunit, 505 amino acids | Propionibacterium freudenreichii subsp. shermanii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-methylmalonyl-CoA + pyruvate | Propionibacterium freudenreichii subsp. shermanii | - |
propanoyl-CoA + oxaloacetate | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Propionibacterium freudenreichii subsp. shermanii | - |
- |
- |
| Propionibacterium freudenreichii subsp. shermanii | - |
Propionibacterium f. shermanii | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant 5S subunit, single step purification using Intein mediated protein ligation method and cleavage from beads by dithiothreitol | Propionibacterium freudenreichii subsp. shermanii |
| the expressed 5S subunit is purified to apparent homogeneity by a single step process by using Intein mediated protein ligation method | Propionibacterium freudenreichii subsp. shermanii |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -70°C, recombinant 5S subunit purified using Intein mediated protein ligation method and cleavage from beads by dithiothreitol, stable for months | Propionibacterium freudenreichii subsp. shermanii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-methylmalonyl-CoA + pyruvate | - |
Propionibacterium freudenreichii subsp. shermanii | propanoyl-CoA + oxaloacetate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit | Propionibacterium freudenreichii subsp. shermanii |
| multimer | the central cylindrical hexameric 12S subunit, the outer six dimeric 5S subunit, and the twelve 1.3S linkers | Propionibacterium freudenreichii subsp. shermanii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5S subunit of transcarboxylase | - |
Propionibacterium freudenreichii subsp. shermanii |
| methylmalonyl CoA-oxalacetate transcarboxylase | - |
Propionibacterium freudenreichii subsp. shermanii |
| transcarboxylase | - |
Propionibacterium freudenreichii subsp. shermanii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| biotin | - |
Propionibacterium freudenreichii subsp. shermanii | |
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