ArticleThe Journal of biological chemistry2016
Dimerization of Bacterial Diaminopimelate Decarboxylase Is Essential for Catalysis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Probing the Role of Meso-DAP and Lysine for Growth and Pathogenicity of Pseudomonas aeruginosa.MicrobiologyOpen · 2025Article
- Kinetic and homology model analysis of diaminopimelate decarboxylase from Cyanothece sp. ATCC 51142: unveiling a key enzyme in lysine biosynthesis.Bioscience reports · 2025Article
- Brucellosis in the omics era: integrative perspectives on Brucella genomic architecture, host-pathogen interactions, and disease dynamics.World journal of microbiology & biotechnology · 2025Review
- Transcriptomic characterization of recombinantApplied and environmental microbiology · 2024Article
- Amino Acid Biosynthesis Inhibitors in Tuberculosis Drug Discovery.Pharmaceutics · 2024Review
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Oligomerization engineering of the fluorinase enzyme leads to an active trimer that supports synthesis of fluorometabolites in vitro.Microbial biotechnology · 2022Article
- Thermostable D-amino acid decarboxylases derived from Thermotoga maritima diaminopimelate decarboxylase.Protein engineering, design & selection : PEDS · 2021Article
- An intact membrane is essential for small extracellular vesicle-induced modulation of α-synuclein fibrillization.Journal of extracellular vesicles · 2020Article
- Novel insights into host-pathogen interactions of large yellow croakers (Zoological research · 2020Article
- Ethylicin Prevents Potato Late Blight by Disrupting Protein Biosynthesis ofPathogens (Basel, Switzerland) · 2020Article
- Misfolded α-synuclein causes hyperactive respiration without functional deficit in live neuroblastoma cells.Disease models & mechanisms · 2020Article
- Structure-function analyses of two plantThe Journal of biological chemistry · 2019Article
- Characterization of recombinant dihydrodipicolinate synthase from the bread wheat Triticum aestivum.Planta · 2018Article
- Crystal structure of a SFPQ/PSPC1 heterodimer provides insights into preferential heterodimerization of human DBHS family proteins.The Journal of biological chemistry · 2018Article
- Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.Biophysical reviews · 2018Review
- Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity.The Journal of biological chemistry · 2018Article
- Structure and Function of Cyanobacterial DHDPS and DHDPR.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diaminopimelate decarboxylase (DAPDC) catalyzes the final step in the diaminopimelate biosynthesis pathway of bacteria. The product of the reaction is the essential amino acid l-lysine, which is an important precursor for the synthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria. Accordingly, the enzyme is a promising antibacterial target. Previous structural studies demonstrate that DAPDC exists as monomers, dimers, and tetramers in the crystal state. However, the active oligomeric form has not yet been determined. We show using analytical ultracentrifugation, small angle x-ray scattering, and enzyme kinetic analyses in solution that the active form of DAPDC from Bacillus anthracis, Escherichia coli, Mycobacterium tuberculosis, and Vibrio cholerae is a dimer. The importance of dimerization was probed further by generating dimerization interface mutants (N381A and R385A) of V. cholerae DAPDC. Our studies indicate that N381A and R385A are significantly attenuated in catalytic activity, thus confirming that dimerization of DAPDC is essential for function. These findings provide scope for the development of new antibacterial agents that prevent DAPDC dimerization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.