D-Homocysteine Lactone HCl
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D-Homocysteine Lactone HCl

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

Cyclic Amino Acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
D-Homocysteine Lactone HCl
(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)
Yellow to Brown Powder, Solid or Crystalline Powder
Melting Point
220-224 ℃
Boiling Point
257.1 ℃ at 760 mmHg
Store at -20°C
Soluble in Methanol, DMSO, Water
InChI Key
Canonical SMILES
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.
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