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Literature summary for 2.7.7.7 extracted from

  • Karata, K.; Vaisman, A.; Goodman, M.F.; Woodgate, R.
    Simple and efficient purification of Escherichia coli DNA polymerase V: cofactor requirements for optimal activity and processivity in vitro (2012), DNA Repair, 11, 431-440.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
additional information the DNA polymerase V is comprised by the UmuD'2C protein complex. Pol V activity depends on the beta-clamp and gamma-clamp loaders UmuC and UmuD'2, overview. Pol V shows robust activity on an SSB-coated circular DNA template in the presence of the beta/gamma-complex and a RecA nucleoprotein filament formed in trans Escherichia coli
single-stranded-binding protein SSB protein, Pol V has intrinsically weak DNA polymerase activity, but its catalytic activity can be stimulated in vitro in the presence the beta-processivity clamp, RecA protein bound to ssDNA, and single-stranded-binding protein Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
pol V is encoded in the umuDC operon, expression of His-tagged pol V in Escherichia coli B strain RW644, and expression as His-tagged gamma complex in Escherichia coli strain DV38(lambdaDE3), methd development for co-expression of the UmuD'2C protein complex, modules separately or combined with expression of chaperones DnaK-DnaJ-GrpE (DnaKJE), or DnaKJE with GroESL, overview. His-tagged pol V is highly active in vivo Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information generations of deletion umuDC operon mutants, pol V Mut shows altered requirements of accessory factors compared to the wild-type enzyme, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deoxynucleoside triphosphate + DNAn Escherichia coli
-
 diphosphate + DNAn+1
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinnat His-tagged pol V from Escherichia coli B strain RW644 by nickel affinity chromatography, gel filtration, and hydroxyapatite chromatography, and of His-tagged gamma complex from Escherichia coli strain DV38(lambdaDE3) by nickel affinity chromatography, gel filtration, and anion exxchange chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
-
 Escherichia coli diphosphate + DNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
DNA polymerase V
-
 Escherichia coli
Pol V
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

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

General Information

General Information Comment Organism
additional information the DNA polymerase V is comprised by the UmuD'2C protein complex. Pol V activity depends on the beta-clamp and gamma-clamp loaders UmuC and UmuD'2, overview Escherichia coli
physiological function most damage-induced mutagenesis in Escherichia coli is dependent on pol V Pol V has intrinsically weak DNA polymerase activity, but its catalytic activity can be stimulated in vitro in the presence the beta-processivity clamp, RecA protein bound to ssDNA, and single-stranded-binding (SSB) protein. Processivity of pol V in the presence of accessory factors, overview Escherichia coli