Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 10, Pages 4044-4053
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2017-01-25
DOI
10.1074/jbc.m116.755645
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway
- (2015) Nir Hecht et al. ANALYTICAL BIOCHEMISTRY
- Diversity in ATP concentrations in a single bacterial cell population revealed by quantitative single-cell imaging
- (2014) Hideyuki Yaginuma et al. Scientific Reports
- How good are my data and what is the resolution?
- (2013) Philip R. Evans et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Pupylation as a signal for proteasomal degradation in bacteria
- (2013) Frank Striebel et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Crystal Structure of the Complex between Prokaryotic Ubiquitin-like Protein and Its Ligase PafA
- (2013) Jonas Barandun et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Mycobacterium tuberculosisProkaryotic Ubiquitin-like Protein-deconjugating Enzyme Is an Unusual Aspartate Amidase
- (2012) Kristin E. Burns et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway
- (2012) Dennis Özcelik et al. Nature Communications
- XDS
- (2010) Wolfgang Kabsch ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus
- (2010) Frank Striebel et al. EMBO JOURNAL
- Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway
- (2010) Frank Imkamp et al. EMBO REPORTS
- Prokaryotic Ubiquitin-Like Protein Provides a Two-Part Degron to Mycobacterium Proteasome Substrates
- (2010) K. E. Burns et al. JOURNAL OF BACTERIOLOGY
- Structural Basis for Feedback and Pharmacological Inhibition ofSaccharomyces cerevisiaeGlutamate Cysteine Ligase
- (2010) Ekaterina I. Biterova et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mycobacterial Ubiquitin-like Protein Ligase PafA Follows a Two-step Reaction Pathway with a Phosphorylated Pup Intermediate
- (2010) Ethan Guth et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Prokaryotic Ubiquitin-like Protein (Pup) Is Coupled to Substrates via the Side Chain of Its C-Terminal Glutamate
- (2010) Markus Sutter et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- “Depupylation” of Prokaryotic Ubiquitin-like Protein from Mycobacterial Proteasome Substrates
- (2010) Kristin E. Burns et al. MOLECULAR CELL
- Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
- (2010) Francisca A. Cerda-Maira et al. MOLECULAR MICROBIOLOGY
- ADPase activity of recombinantly expressed thermotolerant ATPases may be caused by copurification of adenylate kinase of Escherichia coli
- (2009) Baoyu Chen et al. FEBS Journal
- A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa
- (2009) Markus Sutter et al. FEBS LETTERS
- Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
- (2009) Bryson D Bennett et al. Nature Chemical Biology
- Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
- (2009) Frank Striebel et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination
- (2008) Lakshminarayan M Iyer et al. Biology Direct
- Proteasomal Protein Degradation in Mycobacteria Is Dependent upon a Prokaryotic Ubiquitin-like Protein
- (2008) Kristin E. Burns et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis
- (2008) M. J. Pearce et al. SCIENCE
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started