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Last update 08 May 2025

Glutamate racemase

Last update 08 May 2025

Basic Info

Synonyms-

Introduction

Provides the (R)-glutamate required for cell wall biosynthesis.

Drugs associated with Glutamate racemase

Pyridodiazepine amine

Target

Glutamate racemase

Mechanism

Glutamate racemase inhibitors

Active Org.

AstraZeneca Pharmaceuticals LP

Originator Org.

AstraZeneca Pharmaceuticals LP

Active Indication

Helicobacter pylori infection

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

NAT304-632018

Target

Glutamate racemase

Mechanism

Glutamate racemase inhibitors

Active Org.

UI College of Pharmacy

Originator Org.

UI College of Pharmacy

Active Indication

Helicobacter pylori infection

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

NAT18-349139

Target

Glutamate racemase

Mechanism

Glutamate racemase inhibitors

Active Org.

UI College of Pharmacy

Originator Org.

UI College of Pharmacy

Active Indication

Helicobacter pylori infection

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with Glutamate racemase

100 Translational Medicine associated with Glutamate racemase

0 Patents (Medical) associated with Glutamate racemase

127

Literatures (Medical) associated with Glutamate racemase

01 Jul 2025·Journal of Microbiological Methods

Development of novel and efficient Corynebacterium glutamicum gene expression systems for industrial enzyme production

Article

Author: Wu, Ziqi ; Xu, Daqing ; Wang, Miao ; Wu, Liqiang ; Ren, Xiaoxin

An ideal microbial gene expression system for industrial enzyme production should possess a function complementary selection marker, a cost-effective inducer, and the ability for extracellular protein secretion. In this study，we employed CRISPR-Cpf1 gene editing technology to construct an engineered Corynebacterium glutamicum host strain, C. glutamicum Δalr∷araE ΔmurI, by deleting the alanine racemase-encoding gene alr and the glutamate racemase-encoding gene murI, and by integrating the Bacillus subtilis arabinose-related compounds permease-encoding gene araE into the chromosome. The two secretion-type expression vectors pAU30S (Sec-type) and pAU30T (Tat-type) that both employ alr as selection marker, the T7 transcription system to transcribe target genes, and the B. subtilis AraR-OR_A1/OR_A2 negative control system to control gene transcription, were constructed. The α-amylase AmyF from Geobacillus stearothermophilus was used as reporter protein to test the applicability of the L-arabinose-induced gene expression systems C. glutamicum/pAU30S and C. glutamicum Δalr∷araE ΔmurI/pAU30T. The results of transparent circle investigation, SDS-PAGE and amylase activity analysis demonstrated that the recombinant AmyF was efficiently expressed and completely secreted into the culture medium in its active form. The C. glutamicum Δalr∷araE ΔmurI/pAU30S and C. glutamicum Δalr∷araE ΔmurI/pAU30T systems represent highly efficient gene expression platforms suitable for the secretory production of industrial enzymes.

23 Apr 2025·Current Topics in Medicinal Chemistry

Superbug Neisseria gonorrhoeae Infections: The Role of the Moonlighting Protein Glutamate Racemase in Treatment and Prevention

Article

Author: Jain, Ravi ; Chaudhry, Uma ; Pandey, Archna ; Kundu, Bishwajit ; Mittal, Avneesh ; Thakur, Sheetal ; Adhana, Sujata ; Sahoo, Sibasis

Introduction:Neisseria gonorrhoeae is a notorious superbug responsible for causing ‘Gonorrhoea’ in humans. Recently, it has been classified as a high-priority pathogen by the World Health Organization due to its increasing resistance to available antibiotics. A multi-prolonged approach is needed to combat the growing problem of drug resistance caused by N. gonorrhoeae. This study evaluates Glutamate Racemase (GR), a moonlighting protein of N. gonorrhoeae (Ng- GR), as a novel therapeutic target with potential for both inhibitor design and peptide vaccine development. Ng-GR plays a crucial role in the peptidoglycan biosynthetic pathway and is highly conserved across bacterial species. Additionally, this protein moonlights to perform a secondary function by binding to DNA gyrase in various organisms.Method:Homology modeling, molecular docking, and molecular dynamics simulations were used to design inhibitors targeting the moonlight function of Ng-GR. The immunogenicity of this protein was assessed using ABCPred-2.0, BepiPred-2.0, and ProPred software.Results:Bisleucocurine A was found to bind at the ectopic site of Ng-GR, disrupting its crucial moonlight function and interfering with the interaction between Ng-GR and N. gonorroheae DNA Gyrase (Ng-gyrase). Interestingly, residues important for its moonlight function were also identified as key immunogenic sites using ABCPred-2.0, BepiPred-2.0, and ProPred software, enhancing the potential of this protein as a vaccine candidate.Conclusion:The GR enzyme’s moonlight function is highlighted as a promising novel target for therapeutic intervention and vaccine development in N. gonorrohoeae.

01 Mar 2025·Infectious Disorders - Drug Targets

Screening and Identification of Natural Compounds as Potential Inhibitors of Glutamate Racemase, an Emerging Drug Target of Food Pathogen E. coli O157:H7: An In-silico Approach to Combat Increasing Drug Resistance

Article

Author: Kumar, Rajnish ; Adhana, Sujata ; Sahoo, Sibasis ; Pandey, Archna ; Faiza, Muniba ; Gupta, Samarth ; Mittal, Avneesh ; Khanna, Anoushka ; Chaudhry, Uma ; Baweja, Renu

Background:Shiga Toxin-Producing Escherichia coli (E. coli O157:H7), capable of causing serious food-borne illnesses, is extensively studied and is known to be transmitted through animal reservoirs or person-to-person contact, leading to severe disease outbreaks. The emergence of antibiotic resistance in these strains, coupled with increased adverse effects of existing therapeutics, underscores the urgent need for alternative therapeutic strategies.Objective:This study aims to evaluate Glutamate Racemase (MurI protein) of the food-path-ogenic E. coli O157:H7 (EC MurI) as a novel drug target. Furthermore, the study seeks to identify new compounds with potential inhibitory effects against this protein.Methods:Using computational tools, the study identified inhibitor binding sites on EC MurI and identified relevant inhibitors capable of binding to these sites. Molecular docking tech-niques were employed to assess potential hits, and selected compounds were further analyzed for their structural activity and binding affinity to the protein.Results:The results of the study revealed that Frigocyclinone and Deslanoside, exhibited the best binding affinity with EC-MurI. Subsequent molecular dynamic (MD) simulations of the selected complexes indicated that both compounds were stable. This suggests that Frigocy-clinone and Deslanoside have the potential to serve as potent inhibitors of EC-MurI.Conclusion:In summary, this study highlights the urgent need for alternative therapies against food-pathogenic E. coli, focusing on E. coli O157:H7. Evaluation of Glutamate Race-mase as a drug target identified Frigocyclinone and Deslanoside as promising inhibitors. MD simulations indicated their stability, suggesting their potential as lead molecules for further research and treatment development.

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Glutamate racemase

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