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Literature summary for 1.8.99.B1 extracted from

  • D'Ambrosio, K.; Pedone, E.; Langella, E.; De Simone, G.; Rossi, M.; Pedone, C.; Bartolucci, S.
    A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics (2006), J. Mol. Biol., 362, 743-752.
    View publication on PubMed
Search for more literature for 1.8.99.B1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown in the presence of 2 M ammonium sulfate, 2% (v/v) PEG 400, 0.1 M Hepes (pH 8). X-ray diffraction data are collected to 1.93 A resolution Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27198
-
 1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy Aeropyrum pernix
27200
-
 gel filtration, electrospray mass spectroscopy Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YDZ4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme reveals an inherent glutathione-dependent thioltransferase activity Aeropyrum pernix ?
-
 ?
[insulin]-disulfide + reduced dithiothreitol
-
 Aeropyrum pernix [insulin]-dithiol + oxidized dithiothreitol
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy Aeropyrum pernix

Synonyms

Synonyms Comment Organism
ApPDO
-
 Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Aeropyrum pernix