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Literature summary for 2.7.7.7 extracted from

  • Balbo, P.B.; Wang, E.C.; Tsai, M.D.
    Kinetic mechanism of active site assembly and chemical catalysis of DNA polymerase beta (2011), Biochemistry, 50, 9865-9875.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ required, substrate-like inhibition by Mg2+ occur, the inhibition is not due to enzyme inactivation, but instead due to the decrease in rate of a step after chemistry Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information transient state kinetic analyses of DNA polymerase beta, stopped flow absorbance assay development and kinetic modeling and simulations, overview. Pre-steady-state kinetic experiments measuring single nucleotide incorporation catalyzed by Pol beta are performed at 37°C, pH 7.1, over a range of both [Mg2+] and [Mg·dATP2?]. Rapid quench kinetics. Kinetics of nucleotide-induced subdomain closing Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, substrate-like inhibition by Mg2+ occur Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information at low pH the chemical step is rate limiting for catalysis, but at high pH, a postchemistry conformational step is rate limiting due to a pH-dependent increase in the rate of nucleotidyl transfer Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
DNA polymerase beta
-
Rattus norvegicus
pol beta
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1 8.9 assay at Rattus norvegicus

General Information

General Information Comment Organism
additional information binding and recognition of the correct dNTP, the recombinant enzyme performs several small steps like local conformational changes involving active site residues, reorganization of Mg2+-coordinating ligands, and proton transfer Rattus norvegicus