3.5.1.119: Pup amidohydrolase
This is an abbreviated version!
For detailed information about Pup amidohydrolase, go to the full flat file.
Word Map on EC 3.5.1.119
-
3.5.1.119
-
ubiquitin-like
-
tuberculosis
-
mycobacterial
-
depupylation
-
actinobacteria
-
isopeptide
-
deamidated
-
ligases
-
pup-proteasome
-
atpase
-
transacylase
-
malonyl
-
doom
-
adp
-
medicine
-
pharmacology
-
drug development
-
analysis
- 3.5.1.119
-
ubiquitin-like
- tuberculosis
-
mycobacterial
-
depupylation
- actinobacteria
-
isopeptide
-
deamidated
- ligases
-
pup-proteasome
- atpase
-
transacylase
-
malonyl
-
doom
- adp
- medicine
- pharmacology
- drug development
- analysis
Reaction
Synonyms
deamidase of Pup, deamidase/depupylase, deamidase/depupylase Dop, depupylase, depupylase Dop, depupylase/deamidase, Dop, DPUP, Pup deamidase, Rv2112, Rv2112c
ECTree
Advanced search results
General Information
General Information on EC 3.5.1.119 - Pup amidohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
malfunction
metabolism
physiological function
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
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
-
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination
metabolism
the enzyme is critical for the full virulence of Mycobacterium tuberculosis
metabolism
the enzyme is involved in targeted proteasomal degradation
metabolism
-
PafA and depupylase Dop are each required for the full virulence of Mycobacterium tuberculosis
metabolism
-
the enzyme is essential for the infectivity of Mycobacterium tuberculosisis
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
metabolism
-
the enzyme is involved in targeted proteasomal degradation
-
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
-
metabolism
-
the enzyme is critical for the full virulence of Mycobacterium tuberculosis
-
metabolism
-
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination
-
the enzyme is involved in pupylation. Pupylation is a signal for proteasomal degradation in bacteria
physiological function
the enzyme is required for full virulence of Mycobacterium tuberculosis
physiological function
the depupylation reaction can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa
physiological function
-
increased levels of Dop rescues pupylated substrates from destruction by removal of Pup
physiological function
-
the Pup-proteasome enzymes are essential for full virulence and persistence in the mammalian host
physiological function
-
the depupylation reaction can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa
-
physiological function
-
the enzyme is involved in pupylation. Pupylation is a signal for proteasomal degradation in bacteria
-
physiological function
-
the enzyme is required for full virulence of Mycobacterium tuberculosis
-