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Literature summary for 5.6.2.3 extracted from

  • Zhang, H.; Zhang, Z.; Yang, J.; He, Z.G.
    Functional characterization of DnaB helicase and its modulation by single-stranded DNA binding protein in Mycobacterium tuberculosis (2014), FEBS J., 281, 1256-1266 .
    View publication on PubMed
Search for more literature for 5.6.2.3

Activating Compound

Activating Compound Comment Organism Structure
single-stranded binding protein the helicase activity of the enzyme is stimulated by single-stranded binding protein at low concentrations Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
single-stranded binding protein the helicase activity of the enzyme is inhibited by single-stranded binding protein at high concentrations Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 1.5 mM used in assay conditions Mycobacterium tuberculosis

Organism

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

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose column chromatography, and Superdex 200 gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme has both helicase activity (5' to 3' DNA unwinding activity) and single-stranded DNA-dependent ATPase activity. ATP and dATP are preferred over the other NTPs and dNTPs. No helicase activity is detected when nonhydrolyzable ADP is added Mycobacterium tuberculosis ?
-
-
additional information the enzyme has both helicase activity (5' to 3' DNA unwinding activity) and single-stranded DNA-dependent ATPase activity. ATP and dATP are preferred over the other NTPs and dNTPs. No helicase activity is detected when nonhydrolyzable ADP is added Mycobacterium tuberculosis H37Rv ?
-
-

Subunits

Subunits Comment Organism
? x * about 50000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
dnaB
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP maximum helicase activity in the presence of 2 mM ATP Mycobacterium tuberculosis