EC Number   |
General Information |
Reference |
|---|
   3.5.1.119 | malfunction |
generation of a dop deletion mutant in Mycobacterium smegmatis. In the Ddop strain, pupylation is severely impaired and the steady-state levels of proteasomal substrate proteins is drastically increased |
-, 730405 |
| 3.5.1.119 | metabolism |
PafA and depupylase Dop are each required for the full virulence of Mycobacterium tuberculosis |
745678 |
| 3.5.1.119 | metabolism |
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination |
-, 730443 |
| 3.5.1.119 | metabolism |
the enzyme is critical for the full virulence of Mycobacterium tuberculosis |
-, 729998 |
| 3.5.1.119 | metabolism |
the enzyme is essential for the infectivity of Mycobacterium tuberculosisis |
752466 |
| 3.5.1.119 | metabolism |
the enzyme is involved in pupylation |
-, 730453 |
| 3.5.1.119 | metabolism |
the enzyme is involved in targeted proteasomal degradation |
-, 730405 |
| 3.5.1.119 | metabolism |
tight Pup binding and the limited degree of interaction of the enzyme (Dop) with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by this enzyme. Under starvation conditions, when accelerated protein pupylation is required, this bias is intensified by depletion of free Dop molecules, thereby minimizing the chance of depupylation. In contrast to Dop (deamidase of Pup), PafA (proteasome accessory factor A), presents a distinct preference for highmolecular-weight protein substrates. As such, PafA and Dop act in concert, rather than canceling each other's activity, to generate a high-molecular-weight pupylome. This bias in pupylome molecular weight distribution is consistent with the proposed nutritional role of the Pup-proteasome system (PPS) under starvation conditions |
-, 746316 |
| 3.5.1.119 | physiological function |
increased levels of Dop rescues pupylated substrates from destruction by removal of Pup |
744607 |
| 3.5.1.119 | physiological function |
the depupylation reaction can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa |
-, 733729 |
