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Literature summary for 3.1.21.2 extracted from

  • Abeldenov, S.; Talhaoui, I.; Zharkov, D.O.; Ishchenko, A.A.; Ramanculov, E.; Saparbaev, M.; Khassenov, B.
    Characterization of DNA substrate specificities of apurinic/apyrimidinic endonucleases from Mycobacterium tuberculosis (2015), DNA Repair, 33, 1-16 .
    View publication on PubMed
Search for more literature for 3.1.21.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kinetic parameters of AP endonucleases from Escherichia coli and Mycobacterium tuberculosis Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
Co2+ the enzyme exhibits a non-linear dependence in the presence of Co2+. The AP site cleavage activity increases from 0.1 to 0.5 mM and then rapidly decreases from 0.5 to 10 mM CoCl2 Mycobacterium tuberculosis
KCl the enzyme requires a low ionic strength Mycobacterium tuberculosis
KCl the enzyme requires high ionic strength, 200 mM KCl Mycobacterium tuberculosis
Mg2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
Mg2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Under pH 7.6 optimal cation concentrations for MtbXthA-catalyzed activities are 2 mM MgCl2 and/or 0.5 mM MnCl2 Mycobacterium tuberculosis
Mn2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Depending on pH, the enzyme requires different concentrations of divalent cations: 0.5 mM MnCl2 at pH 7.6 and 10 mM at pH 6.5. It exhibits a non-linear dependence in the presence of Mn2+. The AP site cleavage activity increases from 0.1 to 0.5 mM and then rapidly decreases from 0.5 to 10 mM MnCl2. 10 mM MnCl2 is optimal Mycobacterium tuberculosis
Mn2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Depending on pH, the enzyme requires different concentrations of divalent cations: 0.5 mM MnCl2 at pH 7.6 and 10 mM at pH 6.5. Under pH 7.6 optimal cation concentrations for MtbXthA-catalyzed activities are 2 mM MgCl2 and/or 0.5 mM MnCl2 Mycobacterium tuberculosis
additional information the presence of Zn2+, Fe2+ and Ni2+ does not significantly stimulate AP endonuclease activity Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30400
-
 calculated from sequence Mycobacterium tuberculosis
33600
-
 calculated from sequence Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P96273
-
-
Mycobacterium tuberculosis P9WQ13
-
-
Mycobacterium tuberculosis H37Rv P96273
-
-
Mycobacterium tuberculosis H37Rv P9WQ13
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double stranded DNA + H2O the enzyme cleaves with good efficiency a DNA duplex containing the abasic site analogue tetrahydrofuran. The enzyme contains apurinic/apyrimidinic endonuclease activity and 3'-5' exonuclease activity Mycobacterium tuberculosis ?
-
 ?
double stranded DNA + H2O the enzyme cleaves with good efficiency a DNA duplex containing the abasic site analogue tetrahydrofuran. The enzyme contains apurinic/apyrimidinic endonuclease activity and 3'-5' exonuclease activity Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

Synonyms Comment Organism
endonuclease IV
-
 Mycobacterium tuberculosis
exonuclease III
-
 Mycobacterium tuberculosis
MtbNfo
-
 Mycobacterium tuberculosis
MtbXthA
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Mycobacterium tuberculosis
60
-
-
 Mycobacterium tuberculosis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 42 25°C: about 35% of maximal activity, 30°C: about 90% of maximal activity, 42°C: about 55% of maximal activity Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kinetic parameters of AP endonucleases from Escherichia coli and Mycobacterium tuberculosis Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Mycobacterium tuberculosis
6.5
-
-
 Mycobacterium tuberculosis

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5 pH 5.5: about 20% of maximal activity, pH 8.5: about 40% of maximal activity Mycobacterium tuberculosis
5.5 6.5 pH 5.5: about 25% of maximal activity, pH 6.5: about 25% of maximal activity Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function key enzyme involved in the repair of abasic sites and DNA strand breaks Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kinetic parameters of AP endonucleases from Escherichia coli and Mycobacterium tuberculosis Mycobacterium tuberculosis