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Literature summary for 2.7.7.7 extracted from

  • Fisher, P.A.
    Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes (1994), Prog. Nucleic Acid Res. Mol. Biol., 47, 371-397.
    View publication on PubMed
Search for more literature for 2.7.7.7

Activating Compound

Activating Compound Comment Organism Structure
proliferating cell nuclear antigen PCNA, specific auxiliary factor stimulating DNA polymerase delta Drosophila melanogaster
proliferating cell nuclear antigen PCNA, specific auxiliary factor stimulating DNA polymerase delta Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ DNA polymerase alpha: free Mg2+ competes with primer for enzyme binding, dramatic inhibition at Mg2+ concentration above the optimum Drosophila melanogaster
Mg2+ DNA polymerase alpha: free Mg2+ competes with primer for enzyme binding, dramatic inhibition at Mg2+ concentration above the optimum Homo sapiens
single-stranded DNA inhibition of polymerase alpha, competitive with respect to activated DNA substrate Drosophila melanogaster
single-stranded DNA inhibition of polymerase alpha, competitive with respect to activated DNA substrate Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ DNA polymerase alpha: increasing concentrations of Mg2+ lead to a dramatically increased affinity for poly(dT) and poly(dC) polypyrimidines, has little or no effect on the interaction of the enzyme with poly(dA) Drosophila melanogaster
Mg2+ DNA polymerase alpha: increasing concentrations of Mg2+ lead to a dramatically increased affinity for poly(dT) and poly(dC) polypyrimidines, has little or no effect on the interaction of the enzyme with poly(dA) Homo sapiens
Mg2+ free Mg2+ competes with primer for enzyme binding, dramatic inhibition at Mg2+ concentration above the optimum, catalytic core binds primer through a Mg2+-chelate, with each of 4 Mg2+ ions acting to coordinate 2 phosphodiester groups Drosophila melanogaster
Mg2+ free Mg2+ competes with primer for enzyme binding, dramatic inhibition at Mg2+ concentration above the optimum, catalytic core binds primer through a Mg2+-chelate, with each of 4 Mg2+ ions acting to coordinate 2 phosphodiester groups Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deoxynucleoside triphosphate + DNAn Drosophila melanogaster DNA polymerase delta: with its auxiliary factor i.e. proliferating cell nuclear antigen, largely responsible for leading-strand synthesis diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn Homo sapiens DNA polymerase delta: with its auxiliary factor i.e. proliferating cell nuclear antigen, largely responsible for leading-strand synthesis diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn Drosophila melanogaster DNA polymerase alpha: with its associated primase largely responsible for lagging-strand synthesis diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn Homo sapiens DNA polymerase alpha: with its associated primase largely responsible for lagging-strand synthesis diphosphate + DNAn+1
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 mechanism Drosophila melanogaster
a
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 mechanism Homo sapiens
a
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 overview: basic mechanism of replicative DNA polymerases alpha and delta Drosophila melanogaster
a
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 overview: basic mechanism of replicative DNA polymerases alpha and delta Homo sapiens
a
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 mechanism of polymerase translocation along templates Drosophila melanogaster
a
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 mechanism of polymerase translocation along templates Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Drosophila melanogaster
-
KB cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn interaction of polymerases with template-primers containing chemically modified or damaged bases Drosophila melanogaster diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn interaction of polymerases with template-primers containing chemically modified or damaged bases Homo sapiens diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn fidelity of DNA replication Drosophila melanogaster diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn fidelity of DNA replication Homo sapiens diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn DNA polymerase delta: with its auxiliary factor i.e. proliferating cell nuclear antigen, largely responsible for leading-strand synthesis Drosophila melanogaster diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn DNA polymerase delta: with its auxiliary factor i.e. proliferating cell nuclear antigen, largely responsible for leading-strand synthesis Homo sapiens diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn DNA polymerase alpha: with its associated primase largely responsible for lagging-strand synthesis Drosophila melanogaster diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn DNA polymerase alpha: with its associated primase largely responsible for lagging-strand synthesis Homo sapiens diphosphate + DNAn+1
-
 ?