4553-17-7

Usage

Uses

Used in Medical Applications:
L-carnitine is utilized as a therapeutic agent for the treatment of various heart and muscle disorders due to its critical role in energy production at the cellular level. It aids in maintaining the proper functioning of cardiac muscles and has been investigated for its potential to improve exercise performance and support weight loss efforts.
Used in Dietary Supplements:
As a dietary supplement, L-carnitine is taken to support overall health and well-being. It is particularly beneficial for individuals who wish to enhance their exercise performance or are looking to lose weight. However, it is crucial to consult a healthcare professional before incorporating L-carnitine supplements into one's regimen, as excessive intake can lead to adverse effects.
Used in the Food Industry:
L-carnitine is also used in the food industry to enhance the nutritional value of certain products. Its presence in the diet can contribute to improved energy metabolism and overall health.

Upstream product

• 7365-90-4 benzyloxycarbonyl-α-benzyl-γ-L-glutamyl-D-glutamic acid dibenzyl ester 
• 7365-91-5 C₃₉H₄₀N₂O₉ 
• 6893-26-1 D-Glutamic acid 
• 449171-15-7 Boc-D-Glu-OEt 
• 23150-65-4 L-glutamic dimethyl ester hydrochloride 
• 86938-17-2 2-(S)-tert-butoxycarbonylaminopentanedioic acid 1-ethyl ester 
• 13515-99-6 D-glutamic acid dimethyl ester hydrochloride 
• 13030-09-6 1-benzyl L-glutamate 
• 56-86-0 L-glutamic acid 
• 3705-42-8 Cbz-(L)-Glu-OBn 
• 2768-50-5 dibenzyl L-glutamate 

Relevant academic research and scientific papers

γ-Glutamyl-dipeptides: Easy tools to rapidly probe the stereoelectronic properties of the ionotropic glutamate receptor binding pocket

γ-Glutamyl-dipeptides, built by condensing the distal carboxylate of L-Glu (or D-Glu) onto a series of differently functionalized amino acids, were prepared and used as tools for rapidly probing the stereo-electronic properties of iGluRs, searching for subtype-selective ligands.

Efficient peptide couplings and their use in the synthesis and isolation of a cyclopenta (G) quinazoline trisodium salt

A new method for the synthesis of L-Glutamyl-γ-D-Glutamic acid and its use in the synthesis of (2R)-((4S)-carboxy-4-(4,N-(((6S)-2-(hydroxymethyl)-4-oxo-3,4,7,8-tetrahydro-3H-cyclopenta[g]quinazolin-6-yl)-N-(prop-2-ynyl)amino)benzamido)butanamido)pentanedioic acid, 1 are provided. Also provided is an efficient method for the isolation and purification of the trisodium salt of the abovementioned acid, 2, in a form suitable for long term storage and use in a parenteral dosing form.

Microstructure of poly(γ-glutamic acid) produced by Bacillus subtilis consisting of clusters of D- and L-glutamic acid repeating units

Poly(γ-glutamic acid) (PGA) produced by a strain of Bacillus subtilis was partially hydrolyzed into various oligopeptides so that the dipeptide fraction was isolated by the preparative thin-layer chromatography. HPLC analysis was applied to the detection of each of the four stereoisomers in this fraction using chemically synthesized authentic samples. The fraction consisted of N-γ-D-glutamyl-D-glutamic acid, N-γ-L-glutamyl-L-glutamic acid, N-γ-D-glutamyl-L-glutamic acid, and N-γ-L-glutamyl-D-glutamic acid at a ratio of 5.9:6.0:1.0:1.0. On the basis of this result, a model was proposed for the microstructure of the bacterial PGA, in which D- and L-glutamic acid repeating units are alternately linked in a single chain of the molecule.

Synthesis of γ-Glutamyl Peptides Catalyzed by Transamidase from Bacillus natto

Crude ammonium sulfate fraction of a cell free extract from Bacillus natto contained an enzyme (or enzymes) which catalyzed the transamidation reaction specific for glutamine.Both L- and D-isomers of glutamine were active as substrate.On incubation of L- or D-glutamine with the enzyme preparation, two peptides consisting of glutamic acid and glutamine were formed.The main component of the peptides was readily isolated by ion-exchange chromatography and identified as γ-glutamylglutamine by paper chromatography and by paper electrophoresis using authentic peptides.The optical configuration of the amino acid residues in the dipeptide was determined by digestion of the acid hydrolyzate with L-glutamic acid decarboxylase, and the result showed that the dipeptide obtained from L-glutamine was a L-L isomer, while the dipeptide from D-glutamine was a D-D isomer.