25520-73-4

Usage

Uses

Used in Pharmaceutical Industry:
(S)-α-Amino-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid is used as an intermediate for the synthesis of tyrosine-derived quinone cofactors, which are essential components in various pharmaceutical applications. These cofactors are involved in numerous biological processes, making them important targets for drug development.
Used in Chemical Synthesis:
In the field of chemical synthesis, (S)-α-Amino-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid serves as a key building block for the creation of various complex organic molecules. Its unique structure allows for further functionalization and modification, leading to the development of novel compounds with potential applications in various industries.
Used in Research and Development:
(S)-α-Amino-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid is also utilized in research and development, particularly in the study of tyrosine-derived quinone cofactors and their role in biological systems. Understanding the properties and reactivity of (S)-α-Amino-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid can contribute to the advancement of scientific knowledge and the discovery of new therapeutic agents.

Upstream product

• 300-48-1 3-O-methyldopa 
• 60-18-4 L-tyrosine 
• 59-92-7 levodopa 

Downstream Products

• 19641-92-0 3-<(R)-2-amino-2-carboxyethylthio>-5-<(S)-2-amino-2-carboxyethyl>-1,2-dihydroxybenzene 
• 55136-58-8 5-S-G-L-D 
• 59-92-7 levodopa 
• 18766-67-1 leucodopachromene 

Relevant academic research and scientific papers

Protection of mesopore-adsorbed organic matter from enzymatic degradation

Synthetic mesoporous alumina and silica minerals with uniform pore geometries, and their nonporous analogues, were used to test the role of mineral mesopores (2-50 nm diameter) in protecting organic matter from enzymatic degradation in soils and sediments

In vitro tyrosinase, acetylcholinesterase, and HSA evaluation of dioxidovanadium (V) complexes: An experimental and theoretical approach

The present study reports the biological evaluation of vanadium(V) complexes (1–3) against three different proteins: tyrosinase, acetylcholinesterase (AChE), and human serum albumin (HSA), which were studied by spectroscopic techniques and molecular docki

Selective determination of L-dopa in the presence of uric acid and ascorbic acid at a gold nanoparticle self-assembled carbon nanotube-modified pyrolytic graphite electrode

Gold nanoparticle-functionalized carbon nanotubes (AuNP-CNT) have been prepared by a novel self-assembly method. The new material has been characterized by transmission electron microscopy (TEM) and X-ray diffraction (XRD) and utilized for constructing Au

Highly sensitive voltammetric sensor based on NiO nanoparticle room temperature ionic liquid modified carbon paste electrode for levodopa analysis

This paper describes the development of 1-methyl-3-butylimidazolium chloride ionic liquid-NiO nanoparticle modified carbon paste electrode (MBICl/NiO/NPs/CPE) for the voltammetric determination of levodopa (l-DOPA) in real samples. We describe the synthes

Probing biocatalytic transformations with CdSe-ZnS QDs

CdSe/ZnS QDs enable the optical probing of the biocatalytic oxidation of tyrosine derivatives and of the scission of peptides by thrombin. CdSe/ZnS QDs were modified with tyrosine methyl ester or with a tyrosine-containing peptide. The tyrosine units were reacted with tyrosinase/O2 to yield the respective l-DOPA and quinone derivatives. The luminescence of QDs modified by the enzyme-generated quinone units is quenched. The quinone-functionalized peptide associated with the QDs was cleaved by thrombin, a process that restored the luminescence of the QDs. Copyright

Reactivity of dinuclear copper(II) complexes towards melanoma cells: Correlation with its stability, tyrosinase mimicking and nuclease activity

In this work, the influence of two new dinuclear copper(II) complexes in the viability of melanoma cells (B16F10 and TM1MNG3) was investigated, with the aim of verifying possible correlations between their cytotoxicity and their structure. One of the comp

Inhibitory effects and molecular mechanism on mushroom tyrosinase by condensed tannins isolation from the fruit of Ziziphus jujuba Mill. var. spinosa (Bunge) Hu ex H. F. Chow

The structure of extracted condensed tannin (CT) from the fruit of Sour jujube (Ziziphus jujuba Mill. var. spinosa (Bunge) Hu ex H. F. Chow) and the molecular mechanisms by which CT inhibits the activity of mushroom tyrosinase were investigated. The structure of CT was characterized by high performance liquid chromatography electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The kinetic assays were used to detect inhibition effect, type and mechanism. UV scanning, fluorescence quenching, copper interacting, o-quinone interaction and molecular docking assays were also used to reveal the molecular mechanisms by which CT inhibit tyrosinase. The results showed the structural units of CT containing afzelechin/epiafzelechin, catechin/epicatechin, and gallocatechin/epigallocatechin. Kinetic analysis showed that CT inhibits both the monophenolase and diphenolase activities of tyrosinase and exhibits reversible, mixed type mechanism. The fruit CT interacts primarily with the copper ions and specific amino acid residue (Asn191, Thr203, Ala202, Ser206, Met201, His194, His54, Glu182 and Ile42) in the active site of tyrosinase to disturb oxidation of substrates by tyrosinase. These results suggested the sour jujube fruit is a potential natural source of tyrosinase inhibitors, and has a potential to be used in food preservation, whitening cosmetics.

Tyrosinase inhibitory polyphenols from roots of Morus Ihou

Twelve polyphenols (1-12) possessing tyrosinase inhibitory properties were isolated from the methanol (95%) extract of Morus Ihou. The isolated compounds consisted of four flavanones (1 -4), four flavones (5-8), and four phenylbenzofuranes (9-12). Moracin derivative 12 proved to be new a compound which was fully characterized. Compounds 1-12 were evaluated for both monophenolase and diphenolase (the two steps catalyzed by tyrosinase) inhibition to identify the structural characteristics required for mushroom tyrosinase inhibition. We observed that all parent compounds (1, 5, and 9) possessing an unsubstituted resorcinol group were highly effective inhibitors of monophenolase activity (IC50 values of 1.3, 1.2, and 7.4 μM). The potency of the inhibitors diminished with alkyl substitution on either the aromatic ring or the hydroxyl functions. Interestingly, flavone 5 was shown to possess only monophenolase inhibitory activity, but flavanone 1 and phenylbenzofuran 9 inhibited diphenolase as well as monophenolase significantly. The inhibitory mode of these species was also dependent upon the skeleton: phenylbenzofuran 9 manifested a simple competitive inhibition mode for monophenolase and diphenolase; on the other hand flavanone 1 (monophenolase, K3 = 0.1966 min-1 μM-1 k4= 0.0082 min ～1, and Kiapp = 0.0468 μM; diphenolase, k3 = 0.0014 min-1 μM-1 k4 = 0.0013 min-1, and Kiapp = 0.8996 μM) and flavone 5 both showed time-dependent inhibition against monophenolase. Compound 1 operated according to the simple reversible slow binding model whereas compound 5 operated under the enzyme isomerization model.

Determining mushroom tyrosinase inhibition by imidazolium ionic liquids: A spectroscopic and molecular docking study

The inhibition effects of imidazolium ionic liquids (ILs) on the enzyme kinetics of mushroom tyrosinase is reported. A simple UV-VIS spectrophotometric assay was used to measure the reaction kinetics of the reaction between mushroom tyrosinase and L-dopa.

Tyrosinase inactivation in its action on dopa

Under aerobic or anaerobic conditions, tyrosinase undergoes a process of irreversible inactivation induced by its physiological substrate l-dopa. Under aerobic conditions, this inactivation occurs through a process of suicide inactivation involving the fo