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Literature summary for 2.7.7.8 extracted from

  • Symmons, M.F.; Jones, G.H.; Luisi, B.F.
    A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation (2000), Structure Fold. Des., 8, 1215-1226.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of gpsI gene encoding PNPase in Escherichia coli Streptomyces antibioticus

Crystallization (Commentary)

Crystallization (Comment) Organism
protein solution mixed at 3/1 ratio with well solution consisting of 2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.5, 5 mM dithiothreitol and 0.75 mM Na2AsO4, crystals are harvested in a so called mirror solution from equilibrated droplets with buffer replacing enzyme solution and no added Na2AsO4, crystals of native PNPase, a tungstate derivative and a seleno-methionyl derivative Streptomyces antibioticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
81132
-
x * 81132, electrospray mass spectrometry Streptomyces antibioticus
81133
-
x * 81133, deduced from nucleotide sequence Streptomyces antibioticus

Organism

Organism UniProt Comment Textmining
Streptomyces antibioticus Q53597
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, HiTrap Q, HiFlow Phenyl-Sepharose Streptomyces antibioticus

Subunits

Subunits Comment Organism
? x * 81133, deduced from nucleotide sequence Streptomyces antibioticus
? x * 81132, electrospray mass spectrometry Streptomyces antibioticus