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Information on EC 3.5.1.119 - Pup amidohydrolase
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EC Tree
3.5.1.119 Pup amidohydrolaseSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
[prokaryotic ubiquitin-like protein]-L-glutamine
+
=
[prokaryotic ubiquitin-like protein]-L-glutamate
+
Synonyms
depupylase, depupylase dop, deamidase of pup, depupylase/deamidase, pup deamidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deamidase of Pup
deamidase/depupylase
deamidase/depupylase Dop
depupylase
depupylase Dop
depupylase/deamidase
Dop
DPUP
Pup deamidase
Rv2112
Rv2112c
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
the enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
the enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
-
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the deamidase activity (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. The enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the deamidase activity (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. The enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
additional information
?
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
enzyme acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes prokaryotic ubiquitin-like protein Pup from substrates by specific cleavage of the isopeptide bond
-
-
?
additional information
?
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
enzyme acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes prokaryotic ubiquitin-like protein Pup from substrates by specific cleavage of the isopeptide bond
-
-
?
additional information
?
-
steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop
-
-
?
additional information
?
-
steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
although the enzyme does not turn over ATP stoichiometrically with substrate, the active site nucleotide species in the enzyme is ADP and inorganic phosphate rather than ATP. Non-hydrolyzable analogs of ATP cannot support the enzymatic reaction
ATP
deamidation requires ATP as a cofactor but not its hydrolysis
ATP
the reaction is ATP-dependent, but ATP is not hydrolyzed during the course of the reaction. Both adenosine-5'-[(alpha,beta)-methylene]triphosphate and adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP), non-hydrolyzable ATP analogues, can substitute for ATP
ATP
although the enzyme does not turn over ATP stoichiometrically with substrate, the active site nucleotide species in the enzyme is ADP and inorganic phosphate rather than ATP. Non-hydrolyzable analogs of ATP cannot support the enzymatic reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme
-
additional information
-
in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes.
Tuberculosis
Mycobacterium tuberculosis Proteasome Accessory Factor A (PafA) Can Transfer Prokaryotic Ubiquitin-Like Protein (Pup) between Substrates.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine
-
pH 8.0, 23°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme
-
additional information
additional information
-
in order to facilitate high-throughput screens for inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
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
-
metabolism
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
-
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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DOP_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
498
0
54574
Swiss-Prot
-
DOP_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
505
0
55179
Swiss-Prot
-
DOP_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
505
0
55179
Swiss-Prot
-
DOP_ACIC1
Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B)
503
0
56577
Swiss-Prot
-
PUP_ACIC1
Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B)
71
0
8105
Swiss-Prot
-
PAFA_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
482
0
53801
Swiss-Prot
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with ATP, protein (Pup) ligase PafA and the depupylase/deamidase Dop are are close structural homologues
structure of full-length Dop, to 2.6 A resolution and to 2.85 A resolution in complex with ATP. The active site is located on the concave surface of the beta-sheet with the nucleotide bound in a deep pocket. A conserved groove leading into the active site could play a role in Pup-binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D95A
E10A
E10A
mutation abolishes Dop activity both in vivo and in vitro
E10A
-
mutation abolishes Dop activity both in vivo and in vitro
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed from isopropyl beta-D-1-thiogalactopyranoside-inducible pET21 vector in Escherichia coli Rosetta
expressed in Escherichia coli ER2566 from plasmid pET11a
recombinant His6-tagged enzyme is highly insoluble when overproduced in Escherichia coli
the dop gene is cloned with a C-terminal His6-tag, expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
-
the Pup-proteasome enzymes are essential for full virulence and persistence in the mammalian host. As such, the Pup-proteasome enzymes are potential targets for development of antituberculosis therapeutics. Such development requires sensitive and robust assays for measurements of enzymatic activities and the effect of examined inhibitors. An in vitro activity assay for Dop, the first enzyme in the Pup-proteasome system is described, that is ased on fluorescence anisotropy measurements. This assay is simple, sensitive, and compatible with a high-throughput format for screening purposes and can be reliably and conveniently used for detailed kinetic measurements of Dop activity
medicine
-
since Dop is necessary for persistent infection by Mycobacterium tuberculosis, its selective inhibition holds potential for tuberculosis therapy
pharmacology
analysis
development of an in vitro activity assay for Dop, based on fluorescence anisotropy measurements. The assay is simple, sensitive, and compatible with a high-throughput format for screening purposes. It can be reliably and conveniently used for detailed kinetic measurements of Dop activity and can be employed with other Dop enzymes
analysis
-
development of an in vitro activity assay for Dop, based on fluorescence anisotropy measurements. The assay is simple, sensitive, and compatible with a high-throughput format for screening purposes. It can be reliably and conveniently used for detailed kinetic measurements of Dop activity and can be employed with other Dop enzymes
-
pharmacology
the enzyme provides an ideal target for the development of selective chemotherapies
pharmacology
-
the enzyme provides an ideal target for the development of selective chemotherapies
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Striebel, F.; Imkamp, F.; zcelik, D.; Weber-Ban, E.
Pupylation as a signal for proteasomal degradation in bacteria
Biochim. Biophys. Acta
1843
103-113
2014
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Burns, K.E.; McAllister, F.E.; Schwerdtfeger, C.; Mintseris, J.; Cerda-Maira, F.; Noens, E.E.; Wilmanns, M.; Hubbard, S.R.; Melandri, F.; Ovaa, H.; Gygi, S.P.; Darwin, K.H.
Mycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase
J. Biol. Chem.
287
37522-37529
2012
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Burns, K.E.; Cerda-Maira, F.A.; Wang, T.; Li, H.; Bishai, W.R.; Darwin, K.H.
"Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates
Mol. Cell.
39
821-827
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Imkamp, F.; Rosenberger, T.; Striebel, F.; Keller, P.M.; Amstutz, B.; Sander, P.; Weber-Ban, E.
Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo
Mol. Microbiol.
75
744-754
2010
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Cerda-Maira, F.A.; Pearce, M.J.; Fuortes, M.; Bishai, W.R.; Hubbard, S.R.; Darwin, K.H.
Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
Mol. Microbiol.
77
1123-1135
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
zcelik, D.; Barandun, J.; Schmitz, N.; Sutter, M.; Guth, E.; Damberger, F.F.; Allain, F.H.; Ban, N.; Weber-Ban, E.
Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway
Nat. Commun.
3
1014
2012
Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus (A0LU49), Acidothermus cellulolyticus ATCC 43068 (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU49)
brenda
Striebel, F.; Imkamp, F.; Sutter, M.; Steiner, M.; Mamedov, A.; Weber-Ban, E.
Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
Nat. Struct. Mol. Biol.
16
647-651
2009
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Hecht, N.; Gur, E.
Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway
Anal. Biochem.
485
97-101
2015
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Imkamp, F.; Striebel, F.; Sutter, M.; Ozcelik, D.; Zimmermann, N.; Sander, P.; Weber-Ban, E.
Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway
EMBO Rep.
11
791-797
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis H37Rv (P9WNU9)
brenda
Zhang, S.; Burns-Huang, K.; Janssen, G.; Li, H.; Ovaa, H.; Hedstrom, L.; Darwin, K.
Mycobacterium tuberculosis proteasome accessory factor A (PafA) can transfer prokaryotic ubiquitin-like protein (Pup) between substrates
mBio
8
e00122-17
2017
Mycolicibacterium smegmatis
brenda
Elharar, Y.; Roth, Z.; Hecht, N.; Rotkopf, R.; Khalaila, I.; Gur, E.
Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system
Proc. Natl. Acad. Sci. USA
113
E1605-E1614
2016
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Hecht, N.; Gur, E.
Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway
Anal. Biochem.
485
97-101
2015
Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus 11B (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU48)
brenda
Eustis, I.C.; Huang, J.; Pilkerton, M.E.; Whedon, S.D.; Chatterjee, C.
A time-resolved Foerster resonance energy transfer assay to measure activity of the deamidase of the prokaryotic ubiquitin-like protein
Anal. Biochem.
487
27-29
2015
Mycobacterium tuberculosis, Corynebacterium glutamicum (Q8NQE1), Corynebacterium glutamicum ATCC 13032 (Q8NQE1)
brenda
Barandun, J.; Damberger, F.; Delley, C.; Laederach, J.; Allain, F.; Weber-Ban, E.
Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
BMC Struct. Biol.
17
1-12
2017
Mycobacterium tuberculosis
brenda
Bolten, M.; Vahlensieck, C.; Lipp, C.; Leibundgut, M.; Ban, N.; Weber-Ban, E.
Depupylase Dop requires inorganic phosphate in the active site for catalysis
J. Biol. Chem.
292
4044-4053
2017
Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus 11B (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU48)
brenda
Laederach, J.; Cui, H.; Weber-Ban, E.
Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation
PLoS ONE
14
e0215439
2019
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
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