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Reference on EC 3.5.1.119 - Pup amidohydrolase

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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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus 11B (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU48), Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Barandun, J.; Damberger, F.F.; Delley, C.L.; Laederach, J.; Allain, F.H.; Weber-Ban, E.
Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
BMC Struct. Biol.
17
doi: 10.1186/s12900-017-0072-1
2017
Mycobacterium tuberculosis
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Corynebacterium glutamicum (Q8NQE1), Corynebacterium glutamicum ATCC 13032 (Q8NQE1), Mycobacterium tuberculosis
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Yoo, J.; Kahne, S.; Darwin, K.
A conserved loop sequence of the proteasome system depupylase Dop regulates substrate selectivity in Mycobacterium tuberculosis
J. Biol. Chem.
298
102478
2022
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis H37Rv (P9WNU9)
Manually annotated by BRENDA team