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Literature summary for 2.7.7.8 extracted from

  • Letendre, C.H.; Singer, M.F.
    Further characterization of the polynucleotide phosphorylase of Micrococcus luteus (1975), Nucleic Acids Res., 2, 149-163.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
enzyme form I is highly susceptible to proteolytic degradation Micrococcus luteus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
71000
-
x * 71000, enzyme form T, enzyme form I shows several bands of different molecular sizes, SDS-PAGE Micrococcus luteus
230000
-
enzyme form T, sedimentation equilibrium ultracentrifugation Micrococcus luteus
270000
-
enzyme form I, sedimentation equilibrium ultracentrifugation Micrococcus luteus

Organism

Organism UniProt Comment Textmining
Micrococcus luteus
-
a primer-independent, i.e. form I enzyme, and a primer-dependent, i.e. form T enzyme
-

Purification (Commentary)

Purification (Comment) Organism
phosphocellulose chromatography, enzyme forms I and T Micrococcus luteus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNAn + a nucleoside diphosphate
-
Micrococcus luteus RNAn+1 + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 71000, enzyme form T, enzyme form I shows several bands of different molecular sizes, SDS-PAGE Micrococcus luteus