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Literature summary for 4.2.99.18 extracted from

  • Vidal, A.E.; Harkiolaki, M.; Gallego, C.; Castillo-Acosta, V.M.; Ruiz-Perez, L.M.; Wilson, K.; Gonzalez-Pacanowska, D.
    Crystal structure and DNA repair activities of the AP endonuclease from Leishmania major (2007), J. Mol. Biol., 373, 827-838.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
into the pET28a vector for expression in Escherichia coli BL21DE3 cells, into the pKK223-3 vector for transformation into the BW528 strain for subsequent complementation studies Leishmania major

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are produced in hanging drops, the structure is solved at a resolution of 2.5 A Leishmania major

Protein Variants

Protein Variants Comment Organism
D335N mutant retains its capacity to bind to AP sites in DNA, but loses its endonuclease activity Leishmania major

Inhibitors

Inhibitors Comment Organism Structure
EDTA incision activity is completely abolished when 10 mM EDTA is added to the reaction Leishmania major

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
-
Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major O15922
-
-

Purification (Commentary)

Purification (Comment) Organism
using a Ni2+-charged HiTrap Chelating HP column and a gel filtration column Leishmania major

Synonyms

Synonyms Comment Organism
AP endonuclease
-
Leishmania major
apurinic/apyrimidinic endonuclease
-
Leishmania major

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
activity assay Leishmania major

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
activity assay Leishmania major

pH Range

pH Minimum pH Maximum Comment Organism
7 8
-
Leishmania major