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Literature summary extracted from

  • Kumar Bhat, R.; Berger, S.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.1 5S subunit of enzyme Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 the gene encoding the 5S subunit is cloned into the pTXB1 vector Propionibacterium freudenreichii subsp. shermanii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.1 55500
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 55620
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 55623
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 55700
-
5S subunit, 505 amino acids Propionibacterium freudenreichii subsp. shermanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate Propionibacterium freudenreichii subsp. shermanii
-
propanoyl-CoA + oxaloacetate
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
-
-
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
Propionibacterium f. shermanii
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1 recombinant 5S subunit, single step purification using Intein mediated protein ligation method and cleavage from beads by dithiothreitol Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 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

EC Number Storage Stability Organism
2.1.3.1 -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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate
-
Propionibacterium freudenreichii subsp. shermanii propanoyl-CoA + oxaloacetate
-
r

Subunits

EC Number Subunits Comment Organism
2.1.3.1 ? x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 multimer the central cylindrical hexameric 12S subunit, the outer six dimeric 5S subunit, and the twelve 1.3S linkers Propionibacterium freudenreichii subsp. shermanii

Synonyms

EC Number Synonyms Comment Organism
2.1.3.1 5S subunit of transcarboxylase
-
Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 methylmalonyl CoA-oxalacetate transcarboxylase
-
Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 transcarboxylase
-
Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin
-
Propionibacterium freudenreichii subsp. shermanii