21675-61-6

Usage

Uses

Used in Research Studies:
L-LEUCINE-[3,4,5-3H(N)] is used as a research tool for labeling and tracking the metabolism and distribution of amino acids in biological systems. This helps scientists better understand the processes involved in protein synthesis and turnover.
Used in Biochemical Research:
In the field of biochemistry, L-LEUCINE-[3,4,5-3H(N)] is utilized to study the mechanisms of protein synthesis and degradation, providing insights into the fundamental processes of life.
Used in Pharmaceutical Research and Development:
L-LEUCINE-[3,4,5-3H(N)] plays a crucial role in the development of new drugs and therapies, as it aids in the investigation of the effects of potential treatments on protein synthesis and other related metabolic pathways.
Used in Drug Metabolism Studies:
This tritiated amino acid is employed in the study of drug metabolism, helping researchers to understand how different substances interact with proteins and amino acids in the body.
It is important to handle and use L-LEUCINE-[3,4,5-3H(N)] with caution due to its radioactive nature and potential hazards. Proper safety measures should be taken to minimize risks associated with its use.

InChI:InChI=1/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1

Upstream product

• 65451-12-9 (RS)-leucinonitrile 
• 61-90-5 L-leucine 
• 1522-34-5 ethyl 2-acetyl-4-methylpentanoate 
• 872270-41-2 amino-isobutyl-malonic acid diethyl ester 
• 873963-42-9 2-acetylamino-2-cyano-4-methyl-valeric acid ethyl ester 
• 54865-20-2 alanyl=>alanyl=>leucine 
• 135-19-3 β-naphthol 
• 74-90-8 hydrogen cyanide 
• 590-86-3 isovaleraldehyde 
• 151-50-8 potassium cyanide 
• 816-66-0 4-methyl-2-oxopentanoic acid 
• 759-05-7 3-methyl-2-ketobutanoic acid 
• 328-38-1 (R)-leucine 
• 7647-01-0 hydrogenchloride 

Downstream Products

• 2899-43-6 DL-leucine ethyl ester 
• 5625-50-3 cyclo-(Leu-Val) 
• 102129-41-9 N-[(2,4,5-trichloro-phenoxy)-acetyl]-DL-leucine 
• 108272-66-8 N-(4-chloro-benzyloxycarbonyl)-leucine 
• 60889-69-2 N-(N-benzoyl-glycyl)-leucine 
• 42534-05-4 N-carbamoyl-DL-leucine 
• 4071-36-7 ethyl N-acetyl-leucinate 
• 55443-74-8 Propionylleucin 
• 108884-40-8 N-p-tolyloxycarbonyl-DL-leucine 
• 31560-27-7 N,N'-terephthaloyl-di-leucine 
• 82157-53-7 N-[(4-chloro-phenoxy)-acetyl]-DL-leucine 
• 17087-14-8 DL-N--leucin 
• 49659-76-9 N-((E)-2-methyl-3-phenyl-acryloyl)-leucine 

Relevant academic research and scientific papers

Identification of Cyclic Depsipeptides and Their Dedicated Synthetase from Hapsidospora irregularis

Seven cyclic depsipeptides were isolated from Hapsidospora irregularis and structurally characterized as the calcium channel blocker leualacin and six new analogues based on the NMR and HRESIMS data. These new compounds were named leualacins B-G. The absolute configurations of the amino acids and 2-hydroxyisocaproic acids were determined by recording the optical rotation values. Biological studies showed that calcium influx elicited by leualacin F in primary human lobar bronchial epithelial cells involves the TRPA1 channel. Through genome sequencing and targeted gene disruption, a noniterative nonribosomal peptide synthetase was found to be involved in the biosynthesis of leualacin. A comparison of the structures of leualacin and its analogues indicated that the A2 and A4 domains of the leualacin synthetase are substrate specific, while A1, A3, and A5 can accept alternative precursors to yield new molecules.

Involvement of glutamine-238 in the substrate specificity of human laeverin/aminopeptidase Q

Human laeverin/aminopeptidase Q (APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of extravillous trophoblasts. In this study, we examined the significance of Gln-238 of laeverin/APQ, a putative S1 site residue, by site-directed mutagenesis for its enzymatic activity and substrate specificity. Replacement of Gln-238 with Ala caused a significant change in substrate specificity rather than a decrease in enzymatic activity. These results indicate that Gln-238 is important for the substrate specificity of laeverin/APQ. In addition, our data suggest that direct electrostatic interaction between substrate and S1 site of the enzyme is not involved in the mutant enzyme's preference for basic amino acids.

Near-Infrared Fluorescent Probe with Remarkable Large Stokes Shift and Favorable Water Solubility for Real-Time Tracking Leucine Aminopeptidase in Living Cells and in Vivo

Leucine aminopeptidase (LAP) is a kind of proteolytic enzymes and associated closely with pathogenesis of cancer and liver injury. Accurate detection of LAP activity with high sensitivity and selectivity is imperative to detect its distribution and dynamic changes for understanding LAP's function and early diagnosing the disease states. However, fluorescent detection of LAP in living systems is challenging. To date, rarely fluorescent probes have been reported for imaging LAP in vivo. In this study, a novel probe (TMN-Leu) was developed by conjugating a near-infrared dicyanoisophorone derivative fluorophore with LAP activatable l-leucine amide moiety for the first time. TMN-Leu featured large Stokes shift (198 nm), favorable water solubility, ultrasensitive sensitivity (detection limit of ～0.38 ng/mL), good specificity, excellent cell membrane permeability, low toxicity, and a prominent near-infrared emission (658 nm) in response to LAP. TMN-Leu has been successfully applied to track LAP of cancer cells and normal cells, monitor LAP changes in different disease models, and rapidly evaluate LAP inhibitor in cell-based assay. Notably, this probe firstly revealed that HCT116 cells with higher LAP activity were more invasive than LAP siRNA transfected HCT116 cells, suggesting that LAP might serve as an indicator reflecting the intrinsic invasion ability of cancer cells. Finally, TMN-Leu was also employed for in vivo real-time imaging LAP in living tumor-bearing nude mice with low background interference. All together, our probe possesses potential value as a promising tool for diagnostic application, cell-based screening inhibitors and in vivo real-time tracking enzymatic activity in preclinical applications.

(STUDIES ON AI-77s, MICROBIAL PRODUCTS WITH PHARMACOLOGICAL ACTIVITY) STRUCTURES AND THE CHEMICAL NATURE OF AI-77s

The structures of a novel gastroprotective substance AI-77-B and its analogues AI-77-C, D, F and G, which are produced by Bacillus pumilus, are described.Five of the asymmetric centers of AI-77-B have S absolute stereochemistry confirmed by X-ray in combination with chemical studies.

Photolysis of rac-leucine with circularly polarized synchrotron radiation

Amino acids that pass the RNA machinery in living organisms occur in L-configuration. The question on the evolutionary origin of this biomolecular asymmetry remains unanswered to this day. Amino acids were detected in artificially produced interstellar ices, and L-enantiomer-enriched amino acids were identified in CM-type meteorites. This hints at a possible interstellar/circumstellar origin of the amino acids themselves as well as their stereochemical asymmetry. Based upon the current knowledge about the occurrence of circularly-polarized electromagnetic radiation in interstellar environments, we subjected rac-leucine to far-UV circularly-polarized synchrotron radiation. Asymmetric photolysis was followed by an analysis in an enantioselective GC/MS system. Here, we report on an advanced photolysis rate of more than 99% for leucine. The results indicate that high photolysis rates can occur under the chosen conditions, favoring enantioselective photolysis. In 2014, the obtained results will be reexamined by cometary mission Rosetta.

Chemical and Metagenomic Studies of the Lethal Black Band Disease of Corals Reveal Two Broadly Distributed, Redox-Sensitive Mixed Polyketide/Peptide Macrocycles

Black band disease (BBD), a lethal, polymicrobial disease consortium dominated by the cyanobacterium Roseofilum reptotaenium, kills many species of corals worldwide. To uncover chemical signals or cytotoxins that could be important in proliferation of Roseofilum and the BBD layer, we examined the secondary metabolites present in geographically diverse collections of BBD from Caribbean and Pacific coral reefs. Looekeyolide A (1), a 20-membered macrocyclic compound formed by a 16-carbon polyketide chain, 2-deamino-2-hydroxymethionine, and d-leucine, and its autoxidation product looekeyolide B (2) were extracted as major compounds (～1 mg g-1 dry wt) from more than a dozen field-collected BBD samples. Looekeyolides A and B were also produced by a nonaxenic R. reptotaenium culture under laboratory conditions at similar concentrations. R. reptotaenium genomes that were constructed from four different metagenomic data sets contained a unique nonribosomal peptide/polyketide biosynthetic cluster that is likely responsible for the biosynthesis of the looekeyolides. Looekeyolide A, which readily oxidizes to looekeyolide B, may play a biological role in reducing H2O2 and other reactive oxygen species that could occur in the BBD layer as it overgrows and destroys coral tissue.

New C14-surfactin methyl ester from the marine bacterium Bacillus pumilus KMM 456

New C14-surfactin methyl ester and eight earlier described surfactins were isolated from the marine bacterium Bacillus pumilus associated with zoantharia Palythoa sp. The structure of the compounds isolated was established based on the data from amino acid analysis, one- and two-dimensional NMR spectroscopy, and tandem nanoelectrospray mass spectrometry. The absolute configurations of amino acids were determined by Marfey's method. Cytotoxic activity of a number of surfactins with respect to the tumor cells HCT-116 and MDA-MB-231 was studied.

Isolation and characterization of two novel antibacterial cyclic hexapeptides from streptomyces alboflavus 313

Two novel cyclic hexapeptides, designated NW-G08 (1) and NW-G09 (2), were isolated from the fermentation broth of Streptomyces alboflavus 313. Their structures were elucidated on the basis of extensive spectroscopic analysis, MS experiments, and chemical

Natalenamides A–C, cyclic tripeptides from the termite-associated Actinomadura sp. RB99

In recent years, investigations into the biochemistry of insect-associated bacteria have increased. When combined with analytical dereplication processes, these studies provide a powerful strategy to identify structurally and/or biologically novel compounds. Non-ribosomally synthesized cyclic peptides have a broad bioactivity spectrum with high medicinal potential. Here, we report the discovery of three new cyclic tripeptides: natalenamides A–C (compounds 1–3). These compounds were identified from the culture broth of the fungus-growing termite-associated Actinomadura sp. RB99 using a liquid chromatography (LC)/ultraviolet (UV)/mass spectrometry (MS)-based dereplication method. Chemical structures of the new compounds (1–3) were established by analysis of comprehensive spectroscopic methods, including one-dimensional (1H and13C) and two-dimensional (1H-1H-COSY, HSQC, HMBC) nuclear magnetic resonance spectroscopy (NMR), together with high-resolution electrospray ionization mass spectrometry (HR-ESIMS) data. The absolute configurations of the new compounds were elucidated using Marfey’s analysis. Through several bioactivity tests for the tripeptides, we found that compound 3 exhibited significant inhibitory effects on 3-isobutyl-1-methylxanthine (IBMX)-induced melanin production. The effect of compound 3 was similar to that of kojic acid, a compound extensively used as a cosmetic material with a skin-whitening effect.

Mechanochemical Racemization of L-Leucine

On treating a ball-milled mixture of L-leucine and such diluents as silicone dioxide in hydrochloric acid, a part of L-leucine was transformed into D-leucine.