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D-Homocysteine Lactone HCl

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

D-Homocysteine Lactone HCl is one of Cysteine impurities. It has potential anticancer activity against tumor cell growth.

Category

Cyclic Amino Acids

Catalog number

BAT-015038

CAS number

104347-13-9

Molecular Formula

C4H7NO2.HCl

Molecular Weight

137.56

IUPAC Name

(3R)-3-aminooxolan-2-one;hydrochloride

Synonyms

(3R)-3-Aminodihydro-2(3H)-furanone hydrochloride (1:1); (R)-(+)-α-amino-γ-butyrolactone hydrochloride; 2(3H)-Furanone, 3-aminodihydro-, (3R)-, hydrochloride (1:1); (3R)-3-aminotetrahydrofuran-2-one hydrochloride; (R)-2-Amino-4-butyrolactone hydrochloride

Related CAS

51744-82-2 (free base)

Appearance

Yellow to Brown Powder, Solid or Crystalline Powder

Purity

≥95%

Melting Point

220-224 °C

Boiling Point

257.1 °C at 760 mmHg

Storage

Store at -20°C

Solubility

Soluble in Methanol, DMSO, Water

InChI

InChI=1S/C4H7NO2.ClH/c5-3-1-2-7-4(3)6;/h3H,1-2,5H2;1H/t3-;/m1./s1

InChI Key

XBKCXPRYTLOQKS-AENDTGMFSA-N

Canonical SMILES

C1COC(=O)C1N.Cl

D-Homocysteine Lactone HCl, a chemical compound with diverse applications, is at the forefront of biochemical and medical research.

Biochemical Research: Delving into the intricacies of homocysteine metabolism, researchers utilize D-Homocysteine Lactone HCl as a cornerstone in biochemical investigations. This compound sheds light on the role of homocysteine in physiological and pathological conditions, such as cardiovascular diseases and neurodegenerative disorders. Employing it as a vital tool, scientists unravel the biochemical mechanisms underlying homocysteine-related cellular effects.

Drug Development: A pivotal player in pharmacological research, D-Homocysteine Lactone HCl facilitates the screening of potential drug candidates targeting homocysteine metabolism. Through high-throughput screening assays, researchers uncover novel inhibitors or activators of enzymes involved in homocysteine regulation, crucial for developing therapeutic agents to combat diseases linked to elevated homocysteine levels.

Nutritional Studies: In the realm of nutritional research, D-Homocysteine Lactone HCl takes center stage in studying the impact of dietary components on homocysteine levels and metabolism. Scientists investigate the effects of vitamins and nutrients interacting with homocysteine pathways, such as folate and vitamin B6. This knowledge is instrumental in crafting targeted nutritional interventions to manage or prevent health issues related to homocysteine.

Biomarker Analysis: Serving as a gold standard in analytical methods, D-Homocysteine Lactone HCl is a cornerstone for quantifying homocysteine levels in biological samples. Laboratories rely on this compound to calibrate assays, ensuring precise measurement of homocysteine concentrations in plasma, urine, and tissues. This meticulous approach is indispensable for clinical diagnostics and disease monitoring, particularly in conditions where homocysteine serves as a critical biomarker for prognosis and treatment evaluation.

1. Shifting redox states of the iron center partitions CDO between crosslink formation or cysteine oxidation.

Njeri CW;Ellis HR Arch Biochem Biophys. 2014 Sep 15;558:61-9. doi: 10.1016/j.abb.2014.06.001. Epub 2014 Jun 11.

Cysteine dioxygenase (CDO) is a mononuclear iron-dependent enzyme that catalyzes the oxidation of L-cysteine to L-cysteine sulfinic acid. The mammalian CDO enzymes contain a thioether crosslink between Cys93 and Tyr157, and purified recombinant CDO exists as a mixture of the crosslinked and non crosslinked isoforms. The current study presents a method of expressing homogenously non crosslinked CDO using a cell permeative metal chelator in order to provide a comprehensive investigation of the non crosslinked and crosslinked isoforms. Electron paramagnetic resonance analysis of purified non crosslinked CDO revealed that the iron was in the EPR silent Fe(II) form. Activity of non crosslinked CDO monitoring dioxygen utilization showed a distinct lag phase, which correlated with crosslink formation. Generation of homogenously crosslinked CDO resulted in an ∼5-fold higher kcat/Km value compared to the enzyme with a heterogenous mixture of crosslinked and non crosslinked CDO isoforms.

2. Lysine- and cysteine-based protein adductions derived from toxic metabolites of 8-epidiosbulbin E acetate.

Lin D;Wang K;Guo X;Gao H;Peng Y;Zheng J Toxicol Lett. 2016 Dec 15;264:20-28. doi: 10.1016/j.toxlet.2016.10.007. Epub 2016 Nov 2.

Furanoid 8-epidiosbulbin E acetate (EEA) is a major constituent of herbal medicine Dioscorea bulbifera L. (DB), a traditional herbal medicine widely used in Asian nations. Our early studies demonstrated that administration of EEA caused acute hepatotoxicity in mice and the observed toxicity required P450-mediated metabolic activation. Protein modification by reactive metabolites of EEA has been suggested to be an important mechanism of EEA-induced hepatotoxicity. The objectives of the present study were to investigate the interaction of the electrophilic reactive metabolites derived from EEA with lysine and cysteine residues of proteins and to define the correlation of protein adductions of EEA and the hepatotoxicity induced by EEA. EEA-derived cis-enedial was found to modify both lysine and cysteine residues of proteins. The observed modifications increased with the increase in doses administered in the animals. The formation of protein adductions derived from the reactive metabolites of EEA were potentiated by buthionine sulfoximine, but were attenuated by ketoconazole.

3. Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.

Kopka B;Magerl K;Savitsky A;Davari MD;Röllen K;Bocola M;Dick B;Schwaneberg U;Jaeger KE;Krauss U Sci Rep. 2017 Oct 17;7(1):13346. doi: 10.1038/s41598-017-13420-1.

Blue-light absorption by the flavin chromophore in light, oxygen, voltage (LOV) photoreceptors triggers photochemical reactions that lead to the formation of a flavin-cysteine adduct. While it has long been assumed that adduct formation is essential for signaling, it was recently shown that LOV photoreceptor variants devoid of the photoactive cysteine can elicit a functional response and that flavin photoreduction to the neutral semiquinone radical is sufficient for signal transduction. Currently, the mechanistic basis of the underlying electron- (eT) and proton-transfer (pT) reactions is not well understood. We here reengineered pT into the naturally not photoreducible iLOV protein, a fluorescent reporter protein derived from the Arabidopsis thaliana phototropin-2 LOV2 domain. A single amino-acid substitution (Q489D) enabled efficient photoreduction, suggesting that an eT pathway is naturally present in the protein. By using a combination of site-directed mutagenesis, steady-state UV/Vis, transient absorption and electron paramagnetic resonance spectroscopy, we investigate the underlying eT and pT reactions.