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Literature summary for 2.7.7.31 extracted from

  • Ramadan, K.; Maga, G.; Shevelev, I.V.; Villani, G.; Blanco, L.; Hubscher, U.
    Human DNA polymerase lambda possesses terminal deoxyribonucleotidyl transferase activity and can elongate RNA primers: implications for novel functions (2003), J. Mol. Biol., 328, 63-72.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00008
-
DNA 37°C, pH 7.5, primer d(N)36, DNA polymerase lambda Homo sapiens
0.0001
-
DNA 37°C, pH 7.5, primer d(T)20, DNA polymerase lambda Homo sapiens
0.0002
-
DNA 37°C, pH 7.5, primer d(T)200, DNA polymerase lambda Homo sapiens
0.0085
-
dTTP 37°C, pH 7.5, primer d(N)36, DNA polymerase lambda Homo sapiens
0.01
-
dTTP 37°C, pH 7.5, primer d(T)20, DNA polymerase lambda Homo sapiens
0.014
-
dTTP 37°C, pH 7.5, primer d(T)200, DNA polymerase lambda Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1 DNA polymerase lambda has enzymic activity, preferentially adding pyrimidines to 3’-OH ends of DNA oligonucleotides and elongationg RNA primers hybridized to a DNA template Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNA
-
Homo sapiens diphosphate + DNAn+1
-
?
dTTP + DNAn
-
Homo sapiens diphosphate + DNAn+1
-
?