S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
Source S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione at Peptiology
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Summary
S-(N-hydroxy‑N‑bromophenylcarbamoyl)glutathione is a synthetic glutathione derivative employed primarily as a biochemical tool. It mimics the natural substrate S‑D‑lactoylglutathione and acts as a competitive inhibitor of human glyoxalase II, the enzyme that hydrolyses S‑D‑lactoylglutathione in the glyoxalase detoxification pathway. The compound is used in enzymatic assays and structural studies to elucidate the catalytic mechanism and substrate‑binding interactions of glyoxalase II.
Mechanism of Action
The molecule occupies the active‑site cavity of glyoxalase II, which contains a binuclear zinc centre. Its carbonyl carbon is positioned near a zinc‑bound hydroxide ion that serves as the nucleophile in catalysis. A phenolic hydroxyl on Tyr‑175 forms a hydrogen bond with the amide nitrogen of the glutathione moiety, stabilising binding. In the wild‑type enzyme the inhibitor shows a low K i, whereas mutation of Tyr‑175 to phenylalanine markedly reduces affinity, indicating the importance of that hydrogen‑bonding interaction.
What the Research Shows
Two peer‑reviewed studies have characterised this compound. A 1999 crystal‑structure analysis showed the ligand bound in the glyoxalase II active site, coordinated to the zinc ions and positioned for nucleophilic attack, providing a high‑resolution view of enzyme‑substrate interactions. A 2000 mutagenesis study demonstrated that the competitive inhibitor’s K i increased 30‑fold when Tyr‑175 was replaced by phenylalanine, reflecting a slower off‑rate and confirming the role of the Tyr‑175 hydrogen bond. Both papers are limited to in‑vitro enzyme work with purified protein; no cellular or animal data were reported.
Reported Benefits
In research settings the compound serves as a valuable probe of glyoxalase II function, allowing scientists to map the active‑site architecture, assess the contribution of specific residues, and guide the design of more potent inhibitors. Its use in crystallography and kinetic assays has clarified how the enzyme binds glutathione‑based substrates and how the zinc centre participates in catalysis.
Limitations of the Evidence
Evidence is confined to biochemical assays with isolated human glyoxalase II; there are no studies of cellular uptake, metabolic stability, or physiological effects. The compound has not been evaluated for therapeutic potential, toxicity, or pharmacokinetics, and its relevance beyond the laboratory enzyme model remains uncertain.
Safety Considerations
No safety, toxicity, or adverse‑effect data are available for this compound. Because it has only been used in vitro, any extrapolation to living systems would be speculative. Researchers should handle it with standard laboratory safety precautions for chemical reagents, including use of protective equipment and proper waste disposal.
How It Is Administered
S-(N‑hydroxy‑N‑bromophenylcarbamoyl)glutathione is employed in aqueous solution for enzyme kinetic assays or crystal‑soaking experiments. It is typically dissolved in buffered media at micromolar concentrations and added directly to purified glyoxalase II preparations. No formulation for clinical administration exists.
Routes of Administration
No administration routes recorded yet.
Goals & Uses
No goal associations recorded yet.
Contraindications
No contraindications recorded yet.
Adverse Effects
No adverse effects recorded yet.
Drug Interactions
No drug interactions recorded yet.
Population Constraints
No population constraints recorded yet.
Regulatory Status
No regulatory status recorded yet.
Evidence & Sources
- Journal ArticleLowRidderström M, et al.2000-01-01T00:00:00.000000Z
- Journal ArticleLowCameron AD, et al.1999-01-01T00:00:00.000000Z
Frequently Asked Questions
What type of compound is S-(N‑hydroxy‑N‑bromophenylcarbamoyl)glutathione?
It is a synthetic glutathione derivative designed to resemble the natural substrate of glyoxalase II and to act as a competitive inhibitor in biochemical studies.
How does the compound interact with glyoxalase II?
The molecule binds in the enzyme’s active site, coordinating to the binuclear zinc ions and forming a hydrogen bond with Tyr‑175, which together stabilize the inhibitor and reduce catalytic turnover.
Has the compound been tested in animals or humans?
No. All published data involve purified human glyoxalase II in vitro; there are no animal or clinical studies reported.
Can this compound be used as a drug?
Currently it is only a research tool. There is no evidence of safety, efficacy, or regulatory approval for therapeutic use.
What is S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione?
S-(N-hydroxy‑N‑bromophenylcarbamoyl)glutathione is a synthetic glutathione derivative employed primarily as a biochemical tool. It mimics the natural substrate S‑D‑lactoylglutathione and acts as a competitive inhibitor of human glyoxalase II, the enzyme that hydrolyses S‑D‑lactoylglutathione in the glyoxalase detoxification pathway. The compound is used in enzymatic assays and structural studies to elucidate the catalytic mechanism and substrate‑binding interactions of glyoxalase II.