EC Number   |
Activating Compound |
Reference |
|---|
   3.6.4.B8 | DNA |
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). ATPase activity of the SsoRFC-complex is substantially stimulated by the primed homopolymer, whereas no effect is detected in the presence of poly(dA)400. The maximal activation (about tenfold) of the ATP-hydrolyzing activity is measured in the presence of poly(dA)4000-oligo(dT)45 at 140 nM |
725694 |
| 3.6.4.B8 | dsDNA |
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 12fold by dsDNA |
725368 |
| 3.6.4.B8 | more |
clamp substrate PCNA proteins are assayed for stimulation of the ATPase activity of the RFC clamp loader complex in the presence of DNA |
757439 |
| 3.6.4.B8 | proliferating cell nuclear antigen |
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 3fold by Methanosarcina acetivorans proliferating cell nuclear antigen |
725368 |
| 3.6.4.B8 | singly primed single-stranded DNA |
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 58fold by singly primed single-stranded DNA |
725368 |
| 3.6.4.B8 | ssDNA |
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 33fold by ssDNA |
725368 |
