EC Number   |
Reaction |
Reference |
|---|
   3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
active site and substrate binding site structures |
666070 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
active site geometry suggests a two-metal ion-dependent catalytic mechanism |
709140 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
active site residues are Asp10, Gu48, Asp70, His124, Asp134 |
657218 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
active site residues D10, E48, D70, and D134 are involved in metal ion binding, overview |
666037 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
active site structure, substrate binding groove, molecular mechanism for specific RNA*DNA hybrid substrate recognition, binding, and cleavage, a general nuclease activity is necessary for catalysis |
656489 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
Asp10 is critical for activity and involved in binding of divalent metal ion |
657310 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
Asp10, Glu48, Asp70, and Asp134 are involved in catalysis, role of Mn2+ in catalysis, mechanism |
654694 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
Asp149 is essential for catalytic activity, Asp7, Glu8 and Asp112 are invovled in metal ion binding |
654714 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
evolutionary conserved flexible regions are important for catalysis, structure function relationship, enthalpic/entropic compensation mechanism, overview |
666879 |
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester |
four acidic active-site residues of Bst-RNase HIII: Asp97, Glu98, Asp202, and Glu232, substrate binding and site structure, active site structure and reaction mechanism, overview |
666070 |
