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Literature summary extracted from

  • Balasingham, S.; Zegeye, D.; Homberset, H.; Rossi, M.; Laerdahl, J.; Bohr, V.; Tonjum, T.
    Enzymatic activities and DNA substrate specificity of Mycobacterium tuberculosis DNA helicase XPB (2012), PLoS ONE, 7, e36960.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.2.4 expressed in Escherichia coli Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.4 Mg2+
-
 Mycobacterium tuberculosis
5.6.2.4 Mn2+
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.4 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.2.4
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 ATP + H2O
-
 Mycobacterium tuberculosis ADP + phosphate
-
 ?
5.6.2.4 dATP + H2O
-
 Mycobacterium tuberculosis dADP + phosphate
-
 ?
5.6.2.4 additional information Mtb XPB efficiently catalyzes DNA unwinding. Enzyme requires a DNA substrate with a 39 overhang of 15 nucleotides or more. Enzyme is not active on substrates containing a 39 RNA tail. Mtb XPB efficiently catalyzes ATP-independent annealing of complementary DNA strands Mycobacterium tuberculosis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.6.2.4 DNA helicase XPB
-
 Mycobacterium tuberculosis
5.6.2.4 Mtb XPB
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.2.4 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6.2.4 7.5
-
 assay at Mycobacterium tuberculosis