STUDIES ON THE INHIBITION OF GLUTAMIC ACID UTILIZATION IN LACTOBACILLUS PLANTARUM

1962 ◽  
Vol 8 (6) ◽  
pp. 869-873 ◽  
Author(s):  
W. A. Zygmunt ◽  
R. L. Evans ◽  
Homer E. Stavely
Keyword(s):  
Glutamic Acid ◽  
Lactobacillus Plantarum ◽  
Bacterial Growth ◽  
Pyroglutamic Acid ◽  
Inhibition Of Growth ◽  
Acid Antagonist

Eighteen compounds including five novel γ-substituted glutamic acid analogues were tested for inhibition of the utilization of L-glutamic acid by Lactobacillus plantarum. All of the test compounds were found to be less active than DL-methionine sulphoxide, a known glutamic acid antagonist, in inhibiting" the growth of L. plantarum. γ-Methylene-DL-glutamic acid and N-benzyl-α-methyl-DL-pyroglutamic acid were found to be the most active inhibitors of bacterial growth. The inhibition of growth produced by γ-methylene-DL-glutamic acid was readily reversed by L-glutamic acid; whereas the inhibition caused by α-methyl-DL-pyroglutamic acid was more refractory to reversal by L-glutamic acid.

Thermal-induced transformation of glutamic acid to pyroglutamic acid and self-cocrystallization: a charge–density analysis

2022 ◽  
Vol 78 (2) ◽  
Author(s):  
Sehrish Akram ◽  
Arshad Mehmood ◽  
Sajida Noureen ◽  
Maqsood Ahmed
Keyword(s):  
Hydrogen Bonds ◽  
Glutamic Acid ◽  
Single Crystal ◽  
Diffraction Data ◽  
Density Functional ◽  
Quantitative Estimation ◽  
Topological Analysis ◽  
Pyroglutamic Acid ◽  
X Ray Diffraction ◽  
X Ray

Thermal-induced transformation of glutamic acid to pyroglutamic acid is well known. However, confusion remains over the exact temperature at which this happens. Moreover, no diffraction data are available to support the transition. In this article, we make a systematic investigation involving thermal analysis, hot-stage microscopy and single-crystal X-ray diffraction to study a one-pot thermal transition of glutamic acid to pyroglutamic acid and subsequent self-cocrystallization between the product (hydrated pyroglutamic acid) and the unreacted precursor (glutamic acid). The melt upon cooling gave a robust cocrystal, namely, glutamic acid–pyroglutamic acid–water (1/1/1), C5H7NO3·C5H9NO4·H2O, whose structure has been elucidated from single-crystal X-ray diffraction data collected at room temperature. A three-dimensional network of strong hydrogen bonds has been found. A Hirshfeld surface analysis was carried out to make a quantitative estimation of the intermolecular interactions. In order to gain insight into the strength and stability of the cocrystal, the transferability principle was utilized to make a topological analysis and to study the electron-density-derived properties. The transferred model has been found to be superior to the classical independent atom model (IAM). The experimental results have been compared with results from a multipolar refinement carried out using theoretical structure factors generated from density functional theory (DFT) calculations. Very strong classical hydrogen bonds drive the cocrystallization and lend stability to the resulting cocrystal. Important conclusions have been drawn about this transition.

Synthesis of biobased succinimide from glutamic acid via silver-catalyzed decarboxylation

RSC Advances ◽  
2014 ◽  
Vol 4 (52) ◽  
pp. 27541-27544 ◽  
Author(s):  
Jin Deng ◽  
Qiu-Ge Zhang ◽  
Tao Pan ◽  
Qing Xu ◽  
Qing-Xiang Guo ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Pyroglutamic Acid ◽  
Oxidative Decarboxylation ◽  
Silver Catalyst ◽  
Step Procedure

Glutamic acid was transformed into succinimide in a two step procedure involving a dehydration in water to pyroglutamic acid followed by an oxidative decarboxylation using a silver catalyst.

scholarly journals Glutamate Racemase Mutants of Bacillus anthracis

2015 ◽  
Vol 197 (11) ◽  
pp. 1854-1861 ◽  
Author(s):  
So-Young Oh ◽  
Stefan G. Richter ◽  
Dominique M. Missiakas ◽  
Olaf Schneewind
Keyword(s):  
Glutamic Acid ◽  
Bacillus Anthracis ◽  
Causative Agent ◽  
Bacterial Growth ◽  
Bacterial Infections ◽  
Content Type ◽  
Antibiotic Development ◽  
Drug Candidates ◽  
Glutamate Racemase ◽  
Cell Shapes

ABSTRACTd-Glutamate is an essential component of bacterial peptidoglycan and a building block of the poly-γ-d-glutamic acid (PDGA) capsule ofBacillus anthracis, the causative agent of anthrax. Earlier work suggested that two glutamate racemases, encoded byracE1andracE2, are each essential for growth ofB. anthracis, supplyingd-glutamic acid for the synthesis of peptidoglycan and PDGA capsule. Earlier work could not explain, however, why two enzymes that catalyze the same reaction may be needed for bacterial growth. Here, we report that deletion ofracE1orracE2did not prevent growth ofB. anthracisSterne (pXO1+pXO2−), the noncapsulating vaccine strain, or ofB. anthracisAmes (pXO1+pXO2+), a fully virulent, capsulating isolate. While mutants with deletions inracE1andracE2were not viable,racE2deletion delayed vegetative growth ofB. anthracisfollowing spore germination and caused aberrant cell shapes, phenotypes that were partially restored by exogenousd-glutamate. Deletion ofracE1orracE2fromB. anthracisAmes did not affect the production or stereochemical composition of the PDGA capsule. A model is presented wherebyB. anthracis, similar toBacillus subtilis, utilizes two functionally redundant racemase enzymes to synthesized-glutamic acid for peptidoglycan synthesis.IMPORTANCEGlutamate racemases, enzymes that convertl-glutamate tod-glutamate, are targeted for antibiotic development. Glutamate racemase inhibitors may be useful for the treatment of bacterial infections such as anthrax, where the causative agent,B. anthracis, requiresd-glutamate for the synthesis of peptidoglycan and poly-γ-d-glutamic acid (PDGA) capsule. Here we show thatB. anthracispossesses two glutamate racemase genes that can be deleted without abolishing either bacterial growth or PDGA synthesis. These data indicate that drug candidates must inhibit both glutamate racemases, RacE1 and RacE2, in order to blockB. anthracisgrowth and achieve therapeutic efficacy.

scholarly journals Glutamic acid antagonist in the vespid venom.

1993 ◽  
Vol 31 (11) ◽  
pp. 755-760
Author(s):  
KATSUHIRO KONNO
Keyword(s):  
Glutamic Acid ◽  
Acid Antagonist

Influence of Water Activity on Foodborne Bacteria — A Review1

1983 ◽  
Vol 46 (2) ◽  
pp. 142-150 ◽  
Author(s):  
WILLIAM H. SPERBER
Keyword(s):  
Glutamic Acid ◽  
Water Activity ◽  
Bacterial Growth ◽  
Food Systems ◽  
New Technologies ◽  
Compatible Solutes ◽  
Food Products ◽  
Influence Of Water ◽  
Chemical Preservatives ◽  
Reduced Water

The influence of water activity on some characteristics of bacterial growth is presented. Bacteria are able to overcome the plasmolytic effect of reduced water activity by intracellularly accumulating compatible solutes such as glutamic acid or proline. In food systems, water activity is one of several preservative factors which interact to form a preservative system. Other preservative factors considered in this review are temperature, pH, O/R potential and chemical preservatives. Control of water activity in foods is receiving more attention as new food products and new technologies are developed.

Metabolism of 14C-Labeled Glutamic Acid and Pyroglutamic Acid in Animals

1966 ◽  
Vol 55 (10) ◽  
pp. 1147-1149 ◽  
Author(s):  
Winthrop E. Lange ◽  
Edward F. Carey
Keyword(s):  
Glutamic Acid ◽  
Pyroglutamic Acid

scholarly journals Multisyringe Flow Injection Analysis of Tropomyosin Allergens in Shellfish Samples

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5809
Author(s):  
Bruno Coulomb ◽  
Fabien Robert-Peillard ◽  
Najib Ben Ali Gam ◽  
Salwa Sadok ◽  
Jean-Luc Boudenne
Keyword(s):  
Glutamic Acid ◽  
Flow Injection ◽  
Flow Injection Analysis ◽  
Muscle Protein ◽  
Thermal Conversion ◽  
Pyroglutamic Acid ◽  
Fluorimetric Determination ◽  
Multisyringe Flow Injection Analysis ◽  
Shrimp Sample ◽  
Analysis System

This paper presents the development and the application of a multisyringe flow injection analysis system for the fluorimetric determination of the major heat-stable known allergen in shrimp, rPen a 1 (tropomyosin). This muscle protein, made up of 284 amino acids, is the main allergen in crustaceans and can be hydrolyzed by microwave in hydrochloric acid medium to produce glutamic acid, the major amino acid in the protein. Glutamic acid can then be quantified specifically by thermal conversion into pyroglutamic acid followed by chemical derivatization of the pyroglutamic acid formed by an analytical protocol based on an OPA-NAC reagent. Pyroglutamic acid can thus be quantified between 1 and 100 µM in less than 15 min with a detection limit of 1.3 µM. The method has been validated by measurements on real samples demonstrating that the response increases with the increase in the tropomyosin content or with the increase in the mass of the shrimp sample.

Sign in / Sign up

Export Citation Format

Share Document