645-14-7

Usage

Uses

Used in Pharmaceutical Industry:
(1H-IMIDAZOL-4-YL)-ACETALDEHYDE is used as a key intermediate in the synthesis of various pharmaceutical compounds due to its unique chemical properties and ability to form heterocyclic structures, which are often found in biologically active molecules.
Used in Agrochemical Industry:
In the agrochemical sector, (1H-IMIDAZOL-4-YL)-ACETALDEHYDE is utilized as a precursor in the development of new agrochemicals, potentially contributing to the creation of more effective and targeted pesticides or fertilizers.
Used in Materials Science:
(1H-IMIDAZOL-4-YL)-ACETALDEHYDE is employed as a building block in the synthesis of advanced materials, where its imidazole ring can contribute to the formation of novel structures with specific properties for various applications.
Used in Medicinal Chemistry Research:
As a compound with demonstrated antifungal and antimicrobial properties, (1H-IMIDAZOL-4-YL)-ACETALDEHYDE is used in medicinal chemistry research for the discovery and development of new drugs with potential therapeutic applications.
Used in Drug Discovery:
(1H-IMIDAZOL-4-YL)-ACETALDEHYDE's potential biological activities make it a candidate for drug discovery, where it can be further optimized and modified to enhance its pharmacological properties and target specific diseases or conditions.

InChI:InChI=1/C5H6N2O/c8-2-1-5-3-6-4-7-5/h2-4H,1H2,(H,6,7)

Upstream product

• 71-00-1 D,L-histidine 
• 71-00-1 L-histidine 
• 71-00-1 L-histidine 
• 51-45-6 histamine 
• 51-45-6 histamine 
• 56-92-8 histamine dichloride 

Downstream Products

• 51-45-6 histamine 

Relevant academic research and scientific papers

Redox hydrogel-based amperometric bienzyme electrodes for fish freshness monitoring

This work presents the design and optimization of amperometric biosensors for the determination of biogenic amines (e.g., histamine, putrescine, cadaverine, tyramine, cystamine, agmatine, spermidine), commonly present in food products, and their application for monitoring of freshness in fish samples. The biosensors were used as the working electrodes of a three-electrode electrochemical cell of wall-jet type, operated at -50 mV vs Ag/AgCl, in a flow injection system. Two different bienzyme electrode designs were considered, one based on the two enzymes [a newly isolated and purified amine oxidase (AO) and horseradish peroxidase (HRP)] simply adsorbed onto graphite electrodes, and one when they were cross-linked to an Os-based redox polymer. The redox hydrogel-based biosensors showed better biosensors characteristics, i.e., sensitivity of 0.194 A M-1 cm-2 for putrescine and 0.073 A M-1 cm-2 for histamine, and detection limits (calculated as three times the signal-to-noise ratio) of 0.17 μM for putrescine and 0.33 μM for histamine. The optimized redox hydrogel-based biosensors were evaluated in terms of stability and selectivity, and were used for the determination of total amine content in fish samples kept for 10 days in different conditions.

Silver(I) and Copper(II) Catalysis for Oxidation of Histidine by Cerium(IV) in Acid Medium: A Comparative Kinetic Study

The catalytic effect of silver(I) and copper(II) ions on the oxidation of histidine by cerium(IV) in aqueous sulfuric acid solutions was studied spectrophotometrically at a constant ionic strength of 3.0 mol dm?3 and at 25°C. In both uncatalyzed and metal ions-catalyzed paths, the reactions exhibited first-order kinetics with respect to [Ce(IV)] and [catalyst], and fractional first-order dependences with respect to [His] and [H+]. The oxidation rates increased as the ionic strength and dielectric constant of the reactions media increased. The catalytic efficiency of Ag(I) was higher than that of Cu(II). Plausible mechanistic schemes for both uncatalyzed and catalyzed reactions were proposed, and the rate laws associated with the suggested mechanisms were derived. In both cases, the final oxidation products of histidine were identified as 2-imidazole acetaldehyde, ammonium ion, and carbon dioxide. The activation parameters associated with the second-order rate constants were evaluated.

Magnetic nanoparticles loaded on mobile crystalline material-41: Preparation, characterization and application as a novel material for the construction of an electrochemical nanosensor

Herein, we envisage the possibility of preparing stable magnetic mobile crystalline material-41 using cetyltrimethylammonium bromide and Fe 3O4 nanoparticles. The Fe3O4 nanoparticles are incorporated into mobile crystalline material-41 in hydrothermal conditions. The prepared mesoporous sample was characterized by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM) and nitrogen adsorption-desorption techniques. The electrochemical behavior of cadaverine, histamine and putrescine was investigated on magnetic mobile crystalline material-41 (MCM-41-Fe 2O3) modified carbon paste electrodes (CPEs). Due to the very large surface area (1213 m2 g-1) and the remarkable electrocatalytic properties of Fe2O3 nanoparticles, MCM-41-Fe2O3 exhibits potent electrocatalytic activity toward the electrooxidation of some selected biogenic amines. MCM-41-Fe 2O3-CPEs provide new capabilities for electrochemical sensing by combining the advantages of Fe2O3 magnetic nanoparticles and MCM-41 with a very large surface area. The process of oxidation and its kinetics were established by using cyclic voltammetry, chronoamperometry techniques, and also, steady state polarization measurements. The apparent electron transfer rate constant (Ks) and transfer coefficient (α) were determined by cyclic voltammetry and were approximately 6.2 s-1 and 0.48, respectively. The linear concentration ranges of the proposed sensors for cadaverine, histamine and putrescine were 0.1-10, 0.01-0.5 and 0.9-35 μM, respectively. Finally, the applicability of the sensor to the determination of electroactive biogenic amine concentrations in fish samples has been successfully demonstrated.

Oxidative degradation of l-histidine by manganese dioxide (MnO2) nano-colloid in HClO4 medium with/without using TX-100 catalyst: A kinetic approach

The kinetics of the oxidative degradation of l-histidine (His) in perchloric acid medium by freshly prepared manganese dioxide (MnO2) nano-colloid have been investigated with and without using TX-100 catalyst at a constant temperature of 35 °C. The progress of the oxidation reaction was checked by monitoring the decrease in absorbance of MnO2 spectrophotometrically at 360 nm. The reaction was observed to be first order with respect to [MnO2] and fractional with respect to [His] and [HClO4] in both uncatalysed and TX-100-catalysed paths. The catalytic effect of TX-100 on the oxidation reaction has been explained by the Tuncay model. Protonated l-histidine is bound to TX-100 and forms a [TX-100-His] intermediate complex which further reacts with MnO2 and decomposes into the oxidation products: 2-imidazole acetaldehyde, Mn(ii), NH4+ and CO2. On the basis of the kinetics results, a possible reaction mechanism is proposed.

Influence of copper(II) catalyst on the oxidation of l-histidine by platinum(IV) in alkaline medium: A kinetic and mechanistic study

The kinetics of oxidation of l-histidine (His) by platinum(IV) in the absence and presence of copper(II) catalyst was studied using spectrophotometry in alkaline medium at a constant ionic strength of 0.1 mol dm-3 and at 25°C. In both cases, the reactions exhibit a 1:1 stoichiometry ([His]:[PtIV]). The rate of the uncatalyzed reaction is dependent on the first power of each of the concentrations of oxidant, substrate and alkali. The catalyzed path shows a first-order dependence on both [PtIV] and [CuII], but the order with respect to both [His] and [OH-] is less than unity. The rate constants increase with increasing ionic strength and dielectric constant of the medium. The catalyzed reaction has been shown to proceed via formation of a copper(II)-histidine intermediate complex, which reacts with the oxidant by an inner-sphere mechanism leading to decomposition of the complex in the rate-determining step. Platinum(IV) is reduced to platinum(II) by the substrate in a one-step two-electron transfer process. This is followed by other fast steps, giving rise to the oxidation products which were identified as 2-imidazole acetaldehyde, ammonia and carbon dioxide. A tentative reaction mechanism is suggested, and the associated rate laws are deduced. The activation parameters with respect to the slow step of the mechanism are reported and discussed.

Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition

Histamine dehydrogenase from Nocardioides simplex (nHmDH) is a homodimer containing one 6-S-cysteinyl FMN (CFMN) and one [4Fe-4S] cluster per monomer. nHmDH catalyses the oxidative deamination of histamine to ammonia and imidazole acetaldehyde, but histamine inhibits its catalytic activity at high concentrations. We mutated gene-encoded residues (Tyr180, Gly268 and Asp269) near CFMN to understand the biophysical meaning of the substrate inhibition. Three mutants Y180F, G268D/D269C and Y180F/G268D/D269C were expressed by considering the DNA sequence alignment of histamine dehydrogenase from Rhizobium sp. 4-9 (rHmDH), which does not suffer from the substrate inhibition. The Y180F/G268D/D269C mutation to mimic rHmDH successfully suppressed the inhibition, although the catalytic activity decreased. The substrate inhibition was weakened by the Y180F mutation, but G268D/D269C was still susceptible to the inhibition. It was found that it also causes changes in the UV-vis absorption spectra of the substrate-reduced form and the redox potential of the enzymes. The characterization suggests that the thermodynamic preference of the semiquinone form of CFMN in the two-electron-reduced subunit of the enzyme is responsible for the substrate inhibition. However, destabilization of the semiquinone form leads to kinetic hindrance due to the uphill single electron transfer from the fully reduced CFMN to the [4Fe-4S] cluster.

A single amino acid substitution converts a histidine decarboxylase to an imidazole acetaldehyde synthase

Histidine decarboxylase (HDC; EC 4.1.1.22), an enzyme that catalyzes histamine synthesis with high substrate specificity, is a member of the group II pyridoxal 5′-phosphate (PLP) -dependent decarboxylase family. Tyrosine is a conserved residue among group II PLP-dependent decarboxylases. Human HDC has a Y334 located on a catalytically important loop at the active site. In this study, we demonstrated that a HDC Y334F mutant is capable of catalyzing the decarboxylation-dependent oxidative deamination of histidine to yield imidazole acetaldehyde. Replacement of the active-site Tyr with Phe in group II PLP-dependent decarboxylases, including mammalian aromatic amino acid decarboxylase, plant tyrosine/DOPA decarboxylase, and plant tryptophan decarboxylase, is expected to result in the same functional change, given that a Y-to-F substitution at the corresponding residue (number 260) in the HDC of Morganella morganii, another group II PLP-dependent decarboxylase, yielded the same effect. Thus, it was suggested that the loss of the OH moiety from the active-site Tyr residue of decarboxylase uniquely converts the enzyme to an aldehyde synthase.

Development of a novel L-histidine assay method using histamine dehydrogenase and a stable mutant of histidine decarboxylase

L-Histidine analysis is essential in physiological research and clinical applications because L-histidine concentrations in biofluids are associated with various diseases. However, an enzymatic method for L-histidine quantitation has not yet been established. Here, we describe a novel L-histidine quantitation assay using a combination of histidine decarboxylase (HDC) and histamine dehydrogenase (HDH) enzymes. Wild-type HDC is unstable and completely lost its activity within 50 days of storage at 4 °C in solution. We rationally designed a HDC C57S mutant with markedly improved stability (storage at 4 °C for over 200 days) without altering the enzyme's substrate specificity. Together with HDH, the HDC C57S mutant was applied to quantify L-histidine concentrations in human plasma. The assay showed high precision (2.0% inter-assay variation) and high accuracy (5.8% deviation from the results of LC/MS).

Characterization of a new enzyme oxidizing ω-amino group of aminocarboxyric acid, aminoalcohols and amines from Phialemonium sp. AIU 274

A new enzyme exhibiting oxidase activity for ω-aminocarboxylic acids, ω-aminoalcohols, monoamines and diamines was found from a newly isolated fungal strain, Phialemonium sp. AIU 274. The enzyme also oxidized aromatic amines, but not l- and d-amino acids. The Vmax/Km value for hexylamine was higher than those for 6-aminoalcohol and 6-aminhexanoic acid in the aliphatic C6 substrates. In the aliphatic amines, the higher Vmax/Km values were obtained by the longer carbon chain amines. Thus, the enzyme catalyzed oxidative deamination of the ω-amino group in a wide variety of the ω-amino compounds and preferred medium- and long-chain substrates. The oxidase with such broad substrate specificity was first reported here. The enzyme contained copper, and the enzyme activity was strongly inhibited by isoniazid, iproniazid and semicarbazide, but not by clorgyline and pargyline. The enzyme was composed of two identical subunits of 75 kDa.

Inhibitors of tumor progression loci-2 (Tpl2) kinase and tumor necrosis factor α (TNF-α) production: Selectivity and in vivo antiinflammatory activity of novel 8-substituted-4-anilino-6-aminoquinoline-3- carbonitriles

Tumor progression loci-2 (Tpl2) (Cot/MAP3K8) is a serine/threonine kinase in the MAP3K family directly upstream of MEK. Recent studies using Tpl2 knockout mice have indicated an important role for Tpl2 in the lipopolysaccharide (LPS) induced production of