EC Number   |
Reaction |
Reference |
|---|
   3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
active site residue is threonine |
208385 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
catalytic mechanism, the enzyme has a unique catalytic cycle, structure-function analysis overview |
729632 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
catalytic mechanism, the enzyme has a unique catalytic cycle, structure-function analysis overview. The enzyme's N-terminal catalytic His182 functions as a nucleophile (Hisnuc) to attack the 3'-phospho-tyrosyl linkage. This results in dissociation of the tyrosine (and by extension Topo1) from the DNA end and the formation of a enzyme-DNA covalent reaction intermediate via a 3'-phospho-histidyl linkage |
-, 729632 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
catalytic mechanism, the enzyme has a unique catalytic cycle, structure-function analysis overview. The enzyme's N-terminal catalytic His263 functions as a nucleophile (Hisnuc) to attack the 3'-phospho-tyrosyl linkage. This results in dissociation of the tyrosine (and by extension Topo1) from the DNA end and the formation of a enzyme-DNA covalent reaction intermediate via a 3'-phospho-histidyl linkage |
729632 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
enzyme is an exonuclease which needs a free end of an oligonucleotide chain for activity |
208365 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
mechanism |
208385, 208387 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
mechanism, overview |
650905 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
mechanism, transition state |
650838 |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
mode of action |
- |
| 3.1.4.1 | [nucleotide]n + H2O = [nucleotide]m + nucleotide |
PC-1, enzymic activities and regulation of PC-1 |
208379 |
