ArticleJournal of molecular biology2007
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- Microbiota-derived D-amino acids in intestinal homeostasis and inflammatory bowel disease.Inflammation and regeneration · 2026Review
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Mycobacterial Targets for Thiourea Derivatives: Opportunities for Virtual Screening in Tuberculosis Drug Discovery.Current medicinal chemistry · 2024Review
- Genome Analysis Coupled With Transcriptomics Reveals the Reduced Fitness of a Hot Spring CyanobacteriumFrontiers in microbiology · 2022Article
- iTRAQ-based quantitative analysis reveals the mechanism underlying the changes in physiological activity in a glutamate racemase mutant strain of Streptococcus mutans UA159.Molecular biology reports · 2020Article
- Detection of D-glutamate production from the dual Function enzyme, 4-amino-4-deoxychorismate Lyase/D-amino Acid Transaminase, inBio-protocol · 2019Article
- Heterologous expression, purification and biochemical characterization of a glutamate racemase (MurI) fromPeerJ · 2019Article
- Glutamate Racemase Is the Primary Target of β-Chloro-d-Alanine in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2016Article
- Biochemical Characterization of Glutamate Racemase-A New Candidate Drug Target against Burkholderia cenocepacia Infections.PloS one · 2016Article
- Biosynthesis of a Novel Glutamate Racemase Containing a Site-Specific 7-Hydroxycoumarin Amino Acid: Enzyme-Ligand Promiscuity Revealed at the Atomistic Level.ACS central science · 2015Article
- Glutamate Racemase Mutants of Bacillus anthracis.Journal of bacteriology · 2015Article
- Analyses of cobalt-ligand and potassium-ligand bond lengths in metalloproteins: trends and patterns.Journal of molecular modeling · 2014Article
- In silico optimization of a fragment-based hit yields biologically active, high-efficiency inhibitors for glutamate racemase.ChemMedChem · 2013Article
- Flooding enzymes: quantifying the contributions of interstitial water and cavity shape to ligand binding using extended linear response free energy calculations.Journal of chemical information and modeling · 2013Article
- Dynamic dissociating homo-oligomers and the control of protein function.Archives of biochemistry and biophysics · 2012Review
- Characterization of the structure and function of Klebsiella pneumoniae allantoin racemase.Journal of molecular biology · 2011Article
- Nature of allosteric inhibition in glutamate racemase: discovery and characterization of a cryptic inhibitory pocket using atomistic MD simulations and pKa calculations.The journal of physical chemistry. B · 2011Article
- Role of purine biosynthesis in Bacillus anthracis pathogenesis and virulence.Infection and immunity · 2011Article
- Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates.Biochemistry · 2009Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Glutamate racemase (RacE) is responsible for converting l-glutamate to d-glutamate, which is an essential component of peptidoglycan biosynthesis, and the primary constituent of the poly-gamma-d-glutamate capsule of the pathogen Bacillus anthracis. RacE enzymes are essential for bacterial growth and lack a human homolog, making them attractive targets for the design and development of antibacterial therapeutics. We have cloned, expressed and purified the two glutamate racemase isozymes, RacE1 and RacE2, from the B. anthracis genome. Through a series of steady-state kinetic studies, and based upon the ability of both RacE1 and RacE2 to catalyze the rapid formation of d-glutamate, we have determined that RacE1 and RacE2 are bona fide isozymes. The X-ray structures of B. anthracis RacE1 and RacE2, in complex with d-glutamate, were determined to resolutions of 1.75 A and 2.0 A. Both enzymes are dimers with monomers arranged in a "tail-to-tail" orientation, similar to the B. subtilis RacE structure, but differing substantially from the Aquifex pyrophilus RacE structure. The differences in quaternary structures produce differences in the active sites of racemases among the various species, which has important implications for structure-based, inhibitor design efforts within this class of enzymes. We found a Val to Ala variance at the entrance of the active site between RacE1 and RacE2, which results in the active site entrance being less sterically hindered for RacE1. Using a series of inhibitors, we show that this variance results in differences in the inhibitory activity against the two isozymes and suggest a strategy for structure-based inhibitor design to obtain broad-spectrum inhibitors for glutamate racemases.
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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.