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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
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
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
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)
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
Mycobacterium tuberculosis, Corynebacterium glutamicum (Q8NQE1), Corynebacterium glutamicum ATCC 13032 (Q8NQE1)
Manually annotated by BRENDA team
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
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