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Literature summary for 2.7.7.7 extracted from

  • Ramadan, K.; Shevelev, I.V.; Maga, G.; Huebscher, U.
    De novo DNA synthesis by human DNA polymerase l, DNA polymerase m and terminal deoxyribonucleotidyl transferase (2004), J. Mol. Biol., 339, 395-404.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F506G inactive mutant enzyme Homo sapiens
F506R complete loss of de novo DNA synthesis Homo sapiens
Y505A slightly less active in de novo DNA synthesis when compared with wild-type enzyme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ DNA polymerase lambda is not able to perform de novo DNA synthesis in the absence of a metal ion activator. Synthesis of de novo DNA is much stronger with Mn2+ than with Mg2+ Homo sapiens
Mn2+ DNA polymerase lambda is not able to perform de novo DNA synthesis in the absence of a metal ion activator. Synthesis of de novo DNA is much stronger with Mn2+ than with Mg2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn DNA polymerase lambda possesses the ability to synthesise in vitro short fragments of DNA in the absence of a primer-template or even a primer or a template. Amino acid Phe506 of poly lambda is essential for the de novo synthesis Homo sapiens diphosphate + DNAn+1
-
?
deoxynucleoside triphosphate + DNAn DNA polymerase mu possesses the ability to synthesize in vitro short fragments of DNA in the absence of a primer-template or even a primer or a template. Amino acid Phe506 of poly lambda is essential for the de novo synthesis Homo sapiens diphosphate + DNAn+1
-
?

Synonyms

Synonyms Comment Organism
DNA polymerase lambda
-
Homo sapiens
DNA polymerase mu
-
Homo sapiens