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Ligand [prokaryotic ubiquitin-like protein]-L-glutamate

Basic Ligand Information

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine

730004

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine

770717

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine

729308, 730010, 745555, 746316, 744607, 745678, 746202, 744878, 745553, 772929, 774604, 755185, 771711, 774343

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]

729883

-

6.3.1.19

4 entries

In Vivo Product in Enzyme-catalyzed Reactions (23 results)

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Show Natural Product (23 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Bcp protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Bcp protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FabD protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FabD protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FadA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FadA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FusA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FusA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[GlmU protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [GlmU protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Icl protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Icl protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Ino1 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Ino1 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[KasA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [KasA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[LeuD protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [LeuD protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Log protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Log protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Mpa protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Mpa protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Mtra protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [MtrA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[MurA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [MurA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[NuoE protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [NuoE protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PafA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PafA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PanB protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PhoH2 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PhoH2 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[RecA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [RecA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Rv0073 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Rv0073 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Rv2859c protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Rv2859c protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[SahH protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [SahH protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3

-

-

3.5.1.119

22 entries

6.3.1.19

ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine = ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine

-

-

Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Substrate (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [adenylate kinase-His6]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[adenylate kinase-His6]-L-lysine

729641

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [FabD]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[FabD]-L-lysine

745678

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [IdeR]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[IdeR]-L-lysine

746316, 744878

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [inositol 1-phosphate synthetase]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[inositol 1-phosphate synthetase]-L-lysine

745678

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [Log]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[Log]-L-lysine

745678

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine

729641

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [myo-inositol-1-phosphate synthetase]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[myo-inositol-1-phosphate synthetase]-L-lysine

729641

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine

746316, 744607, 746202, 744878, 745553

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [phosphoenolpyruvate-protein phosphotransferase I]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[phosphoenolpyruvate-protein phosphotransferase I]-L-lysine

729641

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [prokaryotic ubiquitin-like protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[prokaryotic ubiquitin-like protein]-L-lysine

744878

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine

730004

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine

729975, 729883, 730010, 770717

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine

729308, 730010, 729975, 729883, 729892, 730453, 745555, 746316, 744607, 745678, 746202, 744878, 745553, 772929, 774604, 755185, 771711, 774343

-

6.3.1.19

ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]

729883

-

6.3.1.19

14 entries

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.119

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

-

-

3.5.1.119

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

-

-

3.5.1.119

N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Bcp protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Bcp protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FabD protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FabD protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FadA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FadA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[FusA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [FusA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[GlmU protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [GlmU protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Icl protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Icl protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Ino1 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Ino1 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[KasA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [KasA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[LeuD protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [LeuD protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Log protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Log protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Mpa protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Mpa protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Mtra protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [MtrA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[MurA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [MurA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[NuoE protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [NuoE protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PafA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PafA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PanB protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[PhoH2 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [PhoH2 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[RecA protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [RecA protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Rv0073 protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Rv0073 protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[Rv2859c protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [Rv2859c protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-gamma-L-glutamyl-[SahH protein]-L-lysine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + [SahH protein]-L-lysine

-

-

3.5.1.119

[prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3

-

-

3.5.1.119

25 entries

6.3.1.19

ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine = ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine

-

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

6.3.1.19

0.0023

-

pH 8.0, 30°C

730010

K_M Value (1 result)

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Show KM Value (1 entry)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

6.3.1.19

0.0014

-

25°C, pH 7.4

729975

References & Links

Literature References (27)

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Show Reference (27 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

729308

23557784

Pupylation as a signal for proteasomal degradation in bacteria

2014

Striebel, F.; Imkamp, F.; Özcelik, D.; Weber-Ban, E.

Biochim. Biophys. Acta

1843

103-113

729641

21738222

Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli

2011

Cerda-Maira, F.A.; McAllister, F.; Bode, N.J.; Burns, K.E., Gygi, S.P.; Darwin, K.H.

EMBO Rep.

12

863-870

729883

20355727

Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate

2010

Sutter, M.; Damberger, F.F.; Imkamp, F.; Allain, F.H.; Weber-Ban, E.

J. Am. Chem. Soc.

132

5610-5612

729892

23402667

Fluorescent probes reveal a minimal ligase recognition motif in the prokaryotic ubiquitin-like protein from Mycobacterium tuberculosis

2013

Smirnov, D.; Dhall, A.; Sivanesam, K.; Sharar, R.J.; Chatterjee, C.

J. Am. Chem. Soc.

135

2887-2890

729975

21081505

Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate

2011

Guth, E.; Thommen, M.; Weber-Ban, E.

J. Biol. Chem.

286

4412-4419

730004

22210775

Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation

2012

Delley, C.L.; Striebel, F.; Heydenreich, F.M.; Özcelik, D.; Weber-Ban, E.

J. Biol. Chem.

287

7907-7914

730010

23471967

Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase

2013

Ofer, N.; Forer, N.; Korman, M.; Vishkautzan, M.; Khalaila, I.; Gur, E.

J. Biol. Chem.

288

11287-11293

730453

19448618

Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes

2009

Striebel, F.; Imkamp, F.; Sutter, M.; Steiner, M.; Mamedov, A.; Weber-Ban, E.

Nat. Struct. Mol. Biol.

16

647-651

744607

28143508

Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins

2017

Barandun, J.; Damberger, F.F.; Delley, C.L.; Laederach, J.; Allain, F.H.; Weber-Ban, E.

BMC Struct. Biol.

17

doi: 10.1186/s12900-017-0072-1

744607

28143508

Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins

2017

Barandun, J.; Damberger, F.F.; Delley, C.L.; Laederach, J.; Allain, F.H.; Weber-Ban, E.

BMC Struct. Biol.

17

1

744878

26277445

A kinetic model for the prevalence of mono- over poly-pupylation

2015

Regev, O.; Roth, Z.; Korman, M.; Khalaila, I.; Gur, E.

FEBS J.

282

4176-4186

744878

26277445

A kinetic model for the prevalence of mono- over poly-pupylation

2015

Regev, O.; Roth, Z.; Korman, M.; Khalaila, I.; Gur, E.

FEBS J.

282

4176-4186

744607

2 entries

744878

2 entries

745553

27497689

An extended loop of the Pup ligase, PafA, mediates interaction with protein targets

2016

Regev, O.; Korman, M.; Hecht, N.; Roth, Z.; Forer, N.; Zarivach, R.; Gur, E.

J. Mol. Biol.

428

4143-4153

745555

28478282

Prokaryotic ubiquitin-like protein and its ligase/deligase enzymes

2017

Delley, C.L.; Mueller, A.U.; Ziemski, M.; Weber-Ban, E.

J. Mol. Biol.

429

3486-3499

745555

28478282

Prokaryotic ubiquitin-like protein and its ligase/deligase enzymes

2017

Delley, C.L.; Mueller, A.U.; Ziemski, M.; Weber-Ban, E.

J. Mol. Biol.

429

3486-3499

745678

28223451

Mycobacterium tuberculosis proteasome accessory factor A (PafA) can transfer prokaryotic ubiquitin-like protein (Pup) between substrates

2017

Zhang, S.; Burns-Huang, K.; Janssen, G.; Li, H.; Ovaa, H.; Hedstrom, L.; Darwin, K.

mBio

8

e00122-17

745678

28223451

Mycobacterium tuberculosis proteasome accessory factor A (PafA) can transfer prokaryotic ubiquitin-like protein (Pup) between substrates

2017

Zhang, S.; Burns-Huang, K.; Janssen, G.; Li, H.; Ovaa, H.; Hedstrom, L.; Darwin, K.

mBio

8

e00122-17

746202

26953889

The mechanism of Mycobacterium smegmatis PafA self-pupylation

2016

Chen, X.; Li, C.; Wang, L.; Liu, Y.; Li, C.; Zhang, J.

PLoS ONE

11

e0151021

746202

26953889

The mechanism of Mycobacterium smegmatis PafA self-pupylation

2016

Chen, X.; Li, C.; Wang, L.; Liu, Y.; Li, C.; Zhang, J.

PLoS ONE

11

e0151021

745555

2 entries

745678

2 entries

746202

2 entries

746316

26951665

Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system

2016

Elharar, Y.; Roth, Z.; Hecht, N.; Rotkopf, R.; Khalaila, I.; Gur, E.

Proc. Natl. Acad. Sci. USA

113

E1605-E1614

755185

31009487

Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation

2019

Laederach, J.; Cui, H.; Weber-Ban, E.

PLoS ONE

14

e0215439

755185

31009487

Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation

2019

Laederach, J.; Cui, H.; Weber-Ban, E.

PLoS ONE

14

e0215439

755185

2 entries

770717

29622495

Identification of serine 119 as an effective inhibitor binding site of M. tuberculosis ubiquitin-like protein ligase PafA using purified proteins and M. smegmatis

2018

Jiang, H.W.; Czajkowsky, D.M.; Wang, T.; Wang, X.D.; Wang, J.B.; Zhang, H.N.; Liu, C.X.; Wu, F.L.; He, X.; Xu, Z.W.; Chen, H.; Guo, S.J.; Li, Y.; Bi, L.J.; Deng, J.Y.; Xie, J.; Pei, J.F.; Zhang, X.E.; Tao, S.C.

EBioMedicine

30

225-236

771711

30547686

The transcription of pafA, encoding the prokaryotic ubiquitin-like protein ligase, is regulated by PafBC

2019

Korman, M.; Elharar, Y.; Fishov, I.; Gur, E.

Future Microbiol.

14

11-21

772929

36100038

A conserved loop sequence of the proteasome system depupylase Dop regulates substrate selectivity in Mycobacterium tuberculosis

2022

Yoo, J.; Kahne, S.; Darwin, K.

J. Biol. Chem.

298

102478

774343

31106455

Multiple layers of regulation determine the cellular levels of the Pup ligase PafA in Mycobacterium smegmatis

2019

Korman, M.; Schlussel, S.; Vishkautzan, M.; Gur, E.

Mol. Microbiol.

112

620-631

774604

34789727

Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation

2021

Cui, H.; Mueller, A.U.; Leibundgut, M.; Tian, J.; Ban, N.; Weber-Ban, E.

Nat. Commun.

12

6635

Links to other databases for [prokaryotic ubiquitin-like protein]-L-glutamate

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