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Literature summary extracted from

  • Wong, A.G.; McBurney, K.L.; Thompson, K.J.; Stickney, L.M.; Mackie, G.A.
    The S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and autoregulation (2013), J. Bacteriol., 195, 2021-2031.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.8 expression of wild-type and mutant enzymes in Escherichia coli strain ENS134-3 from modofied plasmid pAW101 and in beta-galactosidase reporter strain IBPC7322(lambdaGF2), overview Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.8 F635A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 F635A/F638A/H650A site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 F635R/F638R/H650R site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 F638A site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 G570C site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 G570C/V679A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 H650A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 I555T site-directed mutagenesis, the mutant enzyme shows slightly reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 I576A site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 I576A/F638A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 I576T site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 I576T/F638A site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 I576T/T585A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.8 K571L site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 K571Q site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme Escherichia coli
2.7.7.8 additional information construction of domain deletion mutants DELTAKH DELTAS1, DELTAKH, and DELTAS1 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.8 Mg2+ required Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.8 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.8 recombinant wild-type and mutant enzymes from Escherichia coli strain ENS134-3 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.8 additional information
-
 recombinant enzyme activity is measured as repression of beta-galactosidase activity in the reporter expression sytem, RNA binding affinity and in vitro RNA-binding activities of wild-type and mutant enzymes, overview Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.8 RNAn+1 + phosphate substrate is synthetic radiolabeled SL9A RNA Escherichia coli RNAn + a nucleoside diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.8 monomer domain organization of the enzyme monomer, homology modeling with KH domain and S1 domain, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.7.8 PNPase
-
 Escherichia coli
2.7.7.8 polynucleotide phosphorylase
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.8 7.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.8 evolution polynucleotide phosphorylase is a conserved, widely distributed phosphorolytic 3'-5' exoribonuclease Escherichia coli
2.7.7.8 additional information the S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and enzyme autoregulation, modeling of the roles of the KH and S1 domains in PNPase-RNA interactions and in substrate binding, overview Escherichia coli