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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.11.2
-
 Mycobacterium tuberculosis
3.1.21.2
-
 Mycobacterium tuberculosis

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.11.2 Ca2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
3.1.11.2 Mg2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
3.1.11.2 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 Mycobacterium tuberculosis
3.1.21.2 Ca2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
3.1.21.2 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
3.1.21.2 KCl the enzyme requires a low ionic strength Mycobacterium tuberculosis
3.1.21.2 KCl the enzyme requires high ionic strength, 200 mM KCl Mycobacterium tuberculosis
3.1.21.2 Mg2+ the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity Mycobacterium tuberculosis
3.1.21.2 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
3.1.21.2 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
3.1.21.2 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
3.1.21.2 additional information the presence of Zn2+, Fe2+ and Ni2+ does not significantly stimulate AP endonuclease activity Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.21.2 30400
-
 calculated from sequence Mycobacterium tuberculosis
3.1.21.2 33600
-
 calculated from sequence Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.1.11.2 Mycobacterium tuberculosis P96273
-
-
3.1.11.2 Mycobacterium tuberculosis H37Rv P96273
-
-
3.1.21.2 Mycobacterium tuberculosis P96273
-
-
3.1.21.2 Mycobacterium tuberculosis P9WQ13
-
-
3.1.21.2 Mycobacterium tuberculosis H37Rv P96273
-
-
3.1.21.2 Mycobacterium tuberculosis H37Rv P9WQ13
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.11.2
-
 Mycobacterium tuberculosis
3.1.21.2
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.2 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 ?
-
 ?
3.1.21.2 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

EC Number Synonyms Comment Organism
3.1.11.2 exonuclease III
-
 Mycobacterium tuberculosis
3.1.11.2 MtbXthA
-
 Mycobacterium tuberculosis
3.1.21.2 endonuclease IV
-
 Mycobacterium tuberculosis
3.1.21.2 exonuclease III
-
 Mycobacterium tuberculosis
3.1.21.2 MtbNfo
-
 Mycobacterium tuberculosis
3.1.21.2 MtbXthA
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.11.2 37
-
-
 Mycobacterium tuberculosis
3.1.21.2 37
-
-
 Mycobacterium tuberculosis
3.1.21.2 60
-
-
 Mycobacterium tuberculosis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.21.2 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]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.21.2 6
-
-
 Mycobacterium tuberculosis
3.1.21.2 6.5
-
-
 Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.21.2 5.5 8.5 pH 5.5: about 20% of maximal activity, pH 8.5: about 40% of maximal activity Mycobacterium tuberculosis
3.1.21.2 5.5 6.5 pH 5.5: about 25% of maximal activity, pH 6.5: about 25% of maximal activity Mycobacterium tuberculosis

General Information

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

kcat/KM [mM/s]

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