Glutamic Acid-1-semialdehyde, a Hypothetical Intermediate in the Biosynthesis of 5-Aminolevulinic Acid

1987 ◽  
Vol 42 (3) ◽  
pp. 209-214 ◽  
Author(s):  
A. Kah ◽  
D. Dörnemann
Keyword(s):  
Chemical Synthesis ◽  
Glutamic Acid ◽  
Aminolevulinic Acid ◽  
Cyclic Compound ◽  
Pyroglutamic Acid ◽  
Chain Mechanism ◽  
Open Chain

Whether glutamate-1-semialdehyde (G-1-SA) or 4,5 dioxovalerate (DOVA) is the intermedi­ate between glutamate and ALA in the C-5 tetrapyrrol pathway is still a matter of controversy. Since no data characterizing G-1-SA are available it is not possible either to identify G-1-SA as intermediate or a precursor of ALA. Therefore, attempts were made to establish a chemical synthesis of this compound. Two strategies were developed: starting from protected glutamate via an open chain mechanism or from the cyclic compound pyroglutamic acid or derivatives. None of the attempts were successful. Both approaches yielded undefined polymeric products when it was tried to liberate G-1-SA from the last intermediate of the synthesis sequence.

Components of chlorophyll biosynthesis in a barley albina mutant unable to synthesize ?-aminolevulinic acid by utilizing the transfer RNA for glutamic acid

Planta ◽  
1992 ◽  
Vol 188 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Wolfgang R. Hess ◽  
Rudolf Schendel ◽  
Wolfhart R�diger ◽  
Birte Fieder ◽  
Thomas B�rner
Keyword(s):  
Glutamic Acid ◽  
Aminolevulinic Acid ◽  
Chlorophyll Biosynthesis ◽  
Transfer Rna

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.

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.

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.

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