EC Number |
Natural Substrates |
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3.4.21.B30 | more |
the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis |
3.4.21.B30 | more |
UmuD2 undergoes autodigestion at elevated pH |
3.4.21.B30 | more |
enzyme UmuD does not bind DNA. the enzyme UmuD interacts with several components of DNA polymerase III, including the polymerase subunit alpha, the beta clamp and the proofreading subunit epsilon, homology modeling and protein-protein docking analysis, overview. It interacts with the alpha subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site. Enzyme UmuD specifically inhibits binding of DNA polymerase III alpha to ssDNA, UmuD residues D91 and G92 are involved in this interaction, molecular modeling, overview |
3.4.21.B30 | UmuD + H2O |
auto-cleavage of UmuD to UmuD' |
3.4.21.B30 | UmuD2 + H2O |
slow auto-cleavage of UmuD2 to UmuD'2 |
3.4.21.B30 | UmuDAb + H2O |
slow auto-cleavage of UmuDAb to UmuDAb'. UmuDAb undergoes a post-translational, LexA-like cleavage event after DNA damage, possibly to achieve its regulatory action |