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Literature summary extracted from

  • Tranier, S.; Mortier-Barriere, I.; Ilbert, M.; Birck, C.; Iobbi-Nivol, C.; Mejean, V.; Samama, J.P.
    Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA (2002), Protein Sci., 11, 2148-2157.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.3 gene torD, DNA sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) as His-tagged protein Shewanella massilia

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.3 recombinant monomeric, dimeric, and trimeric forms, hanging drop vapour diffusion method, 4°C, 0.001 ml of 1.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, 10 mM DTT, mixed with equal volume of reservoir solution containing 1.6 M ammonium sulfate, 100 mM MES, pH 6.4, 4-6 days, cryoprotection by addition of 15% w/v ethylene glycerol to the reservoir solution, X-ray diffraction structure determination and analysis at 2.42 A resolution Shewanella massilia

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.2.3 cytoplasm
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Shewanella massilia 5737
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Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.3 19500
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
1.7.2.3 24100
-
monomeric form, small-angle X-ray scattering Shewanella massilia
1.7.2.3 24350 24360 monomeric form, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
1.7.2.3 24356
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
1.7.2.3 25000
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
1.7.2.3 27900
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
1.7.2.3 47800
-
dimeric form, small-angle X-ray scattering Shewanella massilia
1.7.2.3 48710
-
dimeric form, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.3 additional information Shewanella massilia enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Shewanella massilia
-
TorD, cytoplasmic chaperone of trimethylamine reductase TorA, EC 1.6.6.9, encoded in the tor operon together with TorA and a pentahemic c-type cytochrome
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.3 recombinant His-tagged monomeric, dimeric, and trimeric forms from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography, and gel filtration for the the monomeric form Shewanella massilia

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 additional information enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently Shewanella massilia ?
-
?

Subunits

EC Number Subunits Comment Organism
1.7.2.3 dimer 2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
1.7.2.3 monomer 1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
1.7.2.3 More enzyme forms multiple and stable oligomeric species, e.g. monomers, dimers, and trimers, analysis by ultracentrifugation, small-angle X-ray scattering, preliminary diffraction, and circular dichroism spectra, interconversion of the native oligomeric forms at pH 3.0 Shewanella massilia

Synonyms

EC Number Synonyms Comment Organism
1.7.2.3 TorD
-
Shewanella massilia

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.3 cytochrome c pentahemic Shewanella massilia