EC Number   |
Inhibitors |
Structure |
|---|
   3.6.1.62 | Co2+ |
supports D10p catalytic activity, but fails to demonstrate a synergistic effect on the enzyme when tested with Mn2+ ions |
   |
| 3.6.1.62 | IMP |
competitive product inhibitor |
|
| 3.6.1.62 | m7G5'ppp5'G |
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA |
|
| 3.6.1.62 | m7G5'ppp5'G |
inhibits decapping at large molar ratios relative to capped RNA substrate |
|
| 3.6.1.62 | m7GDP |
although product inhibition by released m7GDP may occur, the amount of m7GDP released from RNA by X29 in these decapping reactions is well below the amount found to inhibit X29 decapping activity in the assay |
|
| 3.6.1.62 | m7GDP |
inhibits decapping at large molar ratios relative to capped RNA substrate |
|
| 3.6.1.62 | m7GTP |
inhibits decapping at large molar ratios relative to capped RNA substrate |
|
| 3.6.1.62 | Mg2+ |
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145 |
|
| 3.6.1.62 | Mn2+ |
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145 |
|
| 3.6.1.62 | more |
Ca2+ ions can not support D10p activity and does not produce a synergistic activation ofD10p in the presence of Mn2+ |
|
