It has been discovered that serine 176 residue plays a crucial role in increasing the hydrolysis rate of the endonuclease of a consensus sequence containing cytidine.
[10] DNase IV is composed of 185 amino acid residues with magnesium ions acting as a cofactor.
[11] DNase IV prefers to attack native DNA acting as an endonuclease with metal ions either Mg++ or Mn++.
[12] Its TIM beta barrel core surrounded by helices with three metal ions —either three Zn2+ or two Zn2+ and one Mn2+ which plays crucial role in AP excision repair.
[10] Since it does not cleave dsDNA in a processive way, the rate of hydrolysis of this enzyme is faster than native DNA in terms of kinetics.
[1] In human body, DNase IV was required for cleavage of a reaction intermediate generated by template strand displacement during gap-filling.