Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Benzaldehydes”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 703 records · Page 39Linked to original sources
PubMed1989

Enhancement and inhibition of mutation by o-vanillin in Escherichia coli.

2-Hydroxy-3-methoxybenzaldehyde (omicron-vanillin), the antimutagenic effect of which has been reported on mutagenesis induced by 4-nitroquinoline 1-oxide (4NQO) in Escherichia coli WP2s, enhanced N-methyl-N'-nitro-N-nitrosoguanidine (MNNG)-induced mutagenesis in the same strain. A remarkable enhancement of mutagenesis provoked by N-methyl-N-nitrosourea (MNU) was also observed by the addition of omicron-vanillin. No enhancing effect was observed on mutagenesis induced by other mutagens such as methyl methanesulfonate (MMS), dimethylsulfate, N-ethyl-N'-nitro-N-nitrosoguanidine (ENNG), N-ethyl-N-nitrosourea (ENU), ethyl methanesulfonate, diethylsulfate, 4NQO and furylfuramide (AF-2). On the contrary, omicron-vanillin greatly suppressed AF-2- and 4NQO-induced mutagenesis and showed a slight suppressing effect against mutagenesis induced by MMS, ENNG and ENU. One possible explanation for the enhancing effect of omicron-vanillin on the mutagenesis induced by MNNG or MNU in E. coli WP2s may be inhibition of an inducible adaptive response. Among 7 derivatives of omicron-vanillin, 2-hydroxy-3-ethoxy-benzaldehyde, omicron-hydroxybenzaldehyde and m-methoxybenzaldehyde showed an enhancing effect on MNNG-induced mutagenesis.

Benzaldehydes↗
PubMed2006

Abacavir prodrugs: microwave-assisted synthesis and their evaluation of anti-HIV activities.

The synthesis of a new series of abacavir prodrugs involving N2-substitution with various substituted benzaldehyde and ketone derivatives is described. The in vitro anti-HIV activities indicated that compound (3-(2-(4-methylaminobenzylideneamino)-6-(cyclopropylamino)-9H-purin-9-yl)cyclopentyl)methanol (3) was found to be most potent compound with EC50 of 0.05 microM and CC50 of >100 microM with selectivity index of >2000. Compound 3 was found to be 32 times more potent than the parent drug (EC50 of 1.6 microM). At pH 7.4, 37 degrees C, the hydrolytic t1/2 ranged between 120 and 240 min.

Anti-HIV Agents↗
PubMed2005

A ribozyme for the aldol reaction.

Directed in vitro evolution can create RNA catalysts for a variety of organic reactions, supporting the "RNA world" hypothesis, which proposes that metabolic transformations in early life were catalyzed by RNA molecules rather than proteins. Among the most fundamental carbon-carbon bond-forming reactions in nature is the aldol reaction, mainly catalyzed by aldolases that utilize either an enamine mechanism (class I) or a Zn(2+) cofactor (class II). We report on isolation of a Zn(2+)-dependent ribozyme that catalyzes an aldol reaction at its own modified 5' end with a 4300-fold rate enhancement over the uncatalyzed background reaction. The ribozyme can also act as an intermolecular catalyst that transfers a biotinylated benzaldehyde derivative to the aldol donor substrate, coupled to an external hexameric RNA oligonucleotide, supporting the existence of RNA-originated biosynthetic pathways for metabolic sugar precursors and other biomolecules.

Aldehydes↗
PubMed2004

A new non-invasive method for recording the electro-olfactogram using external electrodes.

OBJECTIVE: The aim of this investigation was to explore the possibility of recording the electro-olfactogram (EOG) using external electrodes placed on the root of the nose on either side of the bridge and at the medial termination of the eyebrows. The EOG is considered to be the summated generator potential of olfactory receptor cells and therefore represents peripheral olfactory events. Recording of human EOG is technically difficult due to poor access to the olfactory mucosa and the nasal irritation is tolerated by few subjects. METHODS: The evoked potentials at these sites in response to two odourants, n-amyl acetate and benzaldehyde, were recorded simultaneously with the EOG, recorded conventionally with an intranasal electrode, and the olfactory event-related potential (OERP) recorded using scalp electrodes. RESULTS: The extranasal potential recorded at the root of the nose, 0.5-1 cm below the nasion, 1 cm from the ridge and ipsilateral with the stimulus, had the highest degree of correlation with the intranasal EOG. We refer to this site as N1 (left side) and N2 (right side). Further analysis demonstrated that the latency, the time constant of the rising phase and the amplitude of the evoked potential recorded at N1 also had a higher correlation coefficient with the EOG than did those potentials recorded at other sites. Statistical analysis indicated that the latency and time constant of the response recorded externally at N1 were the same as those of the EOG recorded intranasally. CONCLUSIONS: We conclude that an olfactory evoked potential, with many of the characteristics of the EOG recorded from the olfactory mucosa, can be recorded externally at a site close to the bridge of the nose. SIGNIFICANCE: This non-invasive method of recording the EOG will have benefits for the objective assessment of olfactory function.

Adult↗
PubMed2004

Cleaving of S-mandelonitrile catalyzed by S-hydroxynitrile lyase from Hevea brasiliensis--a kinetic investigation based on the rate curve method.

The progress curves of conversion of racemic-mandelonitrile (R-MN) at different concentrations to benzaldehyde (BA) and hydrogen cyanide (HCN), catalyzed by S-hydroxynitrile lyase from Hevea brasiliensis, together with the enantiomeric excess curves of R-MN are converted into individual progress curves of the S- and R-enantiomers. They reveal that, under the prevailing experimental conditions, the non-enzymatic conversion is sufficiently slow compared to its enzyme-catalyzed counterpart, so that it can be ignored in a simplified analysis. Tikhonov regularization is then used to convert the progress curves of the S-enantiomer into reaction rate curves. These curves are used to determine the rate constants in the rate expression based on a three-step reversible ordered Uni-Bi reaction scheme that describes this enzyme-catalyzed reaction. The resulting rate constants are compared against published data. Some of the problems encountered and their solution are briefly discussed.

Acetonitriles↗
PubMed2005

High-resolution crystal structure of AKR11C1 from Bacillus halodurans: an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.

Aldo-keto reductase AKR11C1 from Bacillus halodurans, a new member of aldo-keto reductase (AKR) family 11, has been characterized structurally and biochemically. The structures of the apo and NADPH bound form of AKR11C1 have been solved to 1.25 A and 1.3 A resolution, respectively. AKR11C1 possesses a novel non-aromatic stacking interaction of an arginine residue with the cofactor, which may favor release of the oxidized cofactor. Our biochemical studies have revealed an NADPH-dependent activity of AKR11C1 with 4-hydroxy-2,3-trans-nonenal (HNE). HNE is a cytotoxic lipid peroxidation product, and detoxification in alkaliphilic bacteria, such as B.halodurans, plays a crucial role in survival. AKR11C1 could thus be part of the detoxification system, which ensures the well being of the microorganism. The very poor activity of AKR11C1 on standard, small substrates such as benzaldehyde or DL-glyeraldehyde is consistent with the observed, very open active site lacking a binding pocket for these substrates. In contrast, modeling of HNE with its aldehyde function suitably positioned in the active site suggests that its elongated hydrophobic tail occupies a groove defined by hydrophobic side-chains. Multiple sequence alignment of AKR11C1 with the highly homologous iolS and YqkF proteins shows a high level of conservation in this putative substrate-binding site. We suggest that AKR11C1 is the first structurally characterized member of a new class of AKRs with specificity for substrates with long aliphatic tails.

Alcohol Oxidoreductases↗
PubMed2003

Toluene exposure increases aminophylline-induced seizure susceptibility in mice.

The effects of toluene on the sensitivity to seizures induced by aminophylline were investigated. Mice were pretreated with an ip injection of corn oil or toluene (100-500 mg/kg) followed by a timed intravenous infusion of aminophylline at various time intervals to assess the seizure thresholds and lethal doses. Toluene increased seizure susceptibility to aminophylline in a dose- and time-dependent manner. Toluene-induced enhancement of seizure susceptibility to aminophylline occurred as early as 30 min and persisted for at least 3 days after a single administration of toluene (500 mg/kg). Treatment of benzaldehyde, one of toluene's metabolites, also showed an increase in the susceptibility to aminophylline. The enhancing effect was also observed in caffeine-induced seizures 1 h, but not 1 day after toluene treatment. These results suggest that individuals with toluene exposure may increase the risk for convulsive and even lethal complications associated with the therapeutic use of aminophylline.

Aminophylline↗
PubMed2000

Inactivation of aldophosphamide by human aldehyde dehydrogenase isozyme 3.

Tumors resistant to chemotherapeutic oxazaphosphorines such as cyclophosphamide often overexpress aldehyde dehydrogenase (ALDH), some isozymes of which catalyze the oxidization of aldophosphamide, an intermediate of cyclophosphamide activation, with formation of inert carboxyphosphamide. Since resistance to oxazaphosphorines can be produced in mammalian cells by transfecting them with the gene for human ALDH isozyme 3 (hALDH3), it seems possible that patients receiving therapy for solid tumors with cyclophosphamide might be protected from myelosuppression by their prior transplantation with autologous bone marrow that has been transduced with a retroviral vector causing overexpression of hALDH3. We investigated whether retroviral introduction of hALDH3 into a human leukemia cell line confers resistance to oxazaphosphorines. This was examined in the polyclonal transduced population, that is, without selecting out high expression clones. hALDH3 activity was 0.016 IU/mg protein in the transduced cells (compared with 2x10(-5) IU/mg in untransduced cells), but there was no detectable resistance to aldophosphamide-generating compounds (mafosfamide or 4-hydroperoxycyclophosphamide). The lack of protection was due, in part, to low catalytic activity of hALDH3 towards aldophosphamide, since, with NAD as cofactor, the catalytic efficiency of homogeneous, recombinant hALDH3 for aldophosphamide oxidation was shown to be about seven times lower than that of recombinant hALDH1. The two polymorphic forms of hALDH3 had identical kinetics with either benzaldehyde or aldophosphamide as substrate. Results of initial velocity measurements were consistent with an ordered sequential mechanism for ALDH1 but not for hALDH3; a kinetic mechanism for the latter is proposed, and the corresponding rate equation is presented.

Aldehyde Dehydrogenase↗
PubMed2001

Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells.

Toxic medium chain length alkanals, alkenals, and 4-hydroxyalkenals that are generated during lipid peroxidation are potential substrates for aldehyde dehydrogenase (ALDH) isoforms. We have developed transgenic cell lines to examine the potential for either human ALDH1A1 or ALDH3A1 to protect against damage mediated by these toxic aldehydes. Using crude cytosols from stably transfected cell lines, these aldehydes were confirmed to be excellent substrates for ALDH3A1, but were poorly oxidized by ALDH1A1. Expression of ALDH3A1 by stable transfection in V79 cells conferred a high level of protection against growth inhibition by the medium-chain length aldehyde substrates with highest substrate activity, including hexanal, trans-2-hexenal, trans-2-octenal, trans-2-nonenal, and 4-hydroxy-2-nonenal (HNE). This was reflected in a parallel ability of ALDH3A1 to prevent depletion of glutathione by these aldehydes. Expression of hALDH3 completely blocked the potent induction of apoptosis by HNE in both V79 cells and in a RAW 264.7 murine macrophage cell line, consistent with the observed total prevention of HNE-protein adduct formation. Structure-activity studies indicated that the rank order of potency for the contributions of HNE functional groups to toxicity was aldehyde >/=C2=C3 double bond>>C4-hydroxyl group. Oxidation of the aldehyde moiety of HNE to a carboxyl by ALDH3A1 expressed in stably transfected cell lines drastically reduced its potency for growth inhibition and apoptosis induction. In contrast, ALDH1A1 expression provided only moderate protection against trans-2-nonenal (t2NE), and none against the other six-nine carbon aldehydes. Neither ALDH1A1 nor ALDH3A1 conferred any protection against acrolein, acetaldehyde, or chloroacetaldehyde. A small degree of protection against malondialdehyde was afforded by ALDH1A1, but not ALDH3A1. Paradoxically, cells expressing ALDH3A1 were 1.5-fold more sensitive to benzaldehyde toxicity than control V79 cells. These studies demonstrate that expression of class 3 ALDH, but not class 1 ALDH, can be an important determinant of cellular resistance to toxicity mediated by aldehydes of intermediate chain length that are produced during lipid peroxidation.

Acetaldehyde↗
PubMed2001

Molecular dynamics simulation of class 3 aldehyde dehydrogenase.

Molecular dynamics (MD) simulation of the rat class 3 aldehyde dehydrogenase (ALDH) with nicotinamide dinucleotide (NAD) cofactors and explicit water molecules are reported. Our results demonstrate that MD simulation using the latest methodologies can maintain the crystal structure of the enzyme, as well as closely reproduce the short timescale dynamics of the enzyme. Furthermore, the examination of the distance between the nucleophilic Cys-243 and the NAD cofactor reveal important fluctuations that could be linked to ALDH catalysis. Finally, our quantum mechanical model of benzaldehyde in the active site of ALDH demonstrates that the enzyme requires only minor conformational changes to be poised for nucleophilic attack on the substrate.

Aldehyde Dehydrogenase↗
PubMed2002

Emission of floral volatiles from Mahonia japonica (Berberidaceae).

Flowering Mahonia japonica plants were subjected to controlled environments and the floral volatiles emitted from whole racemes (laterals) were trapped by Porapak Q adsorbent and analysed by GC-FID. An experiment with photoperiods of 6 and 9 h at constant temperature (10+/-1 degrees C) demonstrated that photoperiod was the stimulus for enhanced emission of most volatiles. Small quantitative differences in emitted fragrance composition were observed between light and dark periods and between plants acclimatised to different photoperiods. Maximum rates of emission occurred in the middle of the light period; aromatic compounds (benzaldehyde, benzyl alcohol and indole) displayed a more rapid increase and subsequent decline compared with monoterpenes (cis- and trans-ocimene and linalool). When the photoperiod was extended from 6 to 9 h, maximum rates of emission continued throughout the additional 3 h. Total emission (microg/h) of volatiles was 2-fold greater in the day-time (DT) (39.7 microg/h) compared with the night-time (NT) (19.8 microgg/h) under a 6 h photoperiod and was not significantly different from total emission under a 9 h photoperiod.

Benzaldehydes↗
PubMed2003

Ozonisation coupled with biological degradation for treatment of phenolic pollutants: a mechanistically based study.

Phenolic acids constitute an important group of pollutants which are reluctant to biological treatment. Solutions containing a mixture of cinnamic acid, p-coumaric acid, caffeic acid and ferulic acid were submitted to ozonisation. Then, the changes in biodegradability along the process were studied by means of respirometry. There is an optimum ozone dosage in the interval 3-5 min of treatment which allows to achieve the maximum increase in biodegradability (more than 10 times) and a high efficiency of the ozonisation process (COD decreases to a half of its initial value). Further ozonisation does not help to increase biodegradability and is clearly disadvantageous. Similar results are obtained with actual samples of olive oil wastewaters. This behaviour is explained based on the formation of highly biodegradable benzaldehydes as key ozonisation intermediates, in the early reaction stages.

Benzaldehydes↗
PubMed2000

Pathway of anthracene modification under simulated solar radiation.

Exposure of polycyclic aromatic hydrocarbons (PAHs) to sunlight results in rapid structural photomodification generally via oxidation reactions. These PAH modification products are in many cases more toxic than their parent compounds. In this study, anthracene (ANT), a rapidly photooxidized PAH, was irradiated with simulated solar radiation (SSR, 100 micromol m(-2) s(-1)) in aqueous solution to examine the photomodification pathway. The photoproducts formed were identified by HPLC. The ANT product profile after 9 h in SSR was very complex, with more than 20 compounds detected. The photoproducts formed were anthraquinones, benzoic acids, benzaldehydes and phenols showing the process to be oxidative in nature. Some of the anthraquinones were themselves subject to photooxidation, and were thus intermediates in the product pathway. The kinetics of ANT photooxidation revealed a pseudo first-order reaction with a half-life of 2 h under the SSR source used. The kinetics of product formation allowed deduction of a probable photomodification pathway. This study indicates that PAH photooxidation products are likely to exist as complex, dynamically changing mixtures in PAH contaminated aquatic environments.

Anthracenes↗
PubMed2004

Monitoring of the antioxidant BHT and its metabolite BHT-CHO in German river water and ground water.

The behavior of anthropogenic polar organic compounds in ground water during infiltration of river water to ground water was studied at the Oderbruch area on the eastern border of Germany. Additionally, waste water sewage treatment works (STWs) discharging their treated waste water into the Oder River and rain water precipitation from the Oderbruch area were investigated. The study was carried out from March 2000 to July 2001 to investigate seasonal variations of the target analytes. Samples were collected from four sites along the Oder River, from 24 ground water monitoring wells located close to the Oder, from one rain water collection station, from two roof runoffs, and from four STWs upstream of the Oderbruch. Results of the investigations of the antioxidant 3,5-di-tert-butyl-4-hydroxy-toluene (BHT) and its degradation product 3,5-di-tert-butyl-4-hydroxy-benzaldehyde (BHT-CHO) are presented. BHT and BHT-CHO were detected in all samples of the Oder River with mean concentrations of 178 and 102 ngl(-1), respectively. BHT and BHT-CHO were also detected in effluent waste water samples from municipal STWs at mean concentrations of 132 and 70 ngl(-1), respectively. Both compounds are discharged into river water directly via treated waste water. In the rain water sample, 308 ngl(-1) of BHT and 155 ngl(-1) of BHT-CHO were measured. Both compounds were detected in roof runoff with mean concentrations of 92 ngl(-1) for BHT and 138 ngl(-1) for BHT-CHO. The median values of BHT and BHT-CHO in ground water samples were 132 and 84 ngl(-1), respectively. The chemical composition of ground water from parts of the aquifer located less than 4.5 m distant from the river are greatly influenced by bank filtration. However, wet deposition followed by seepage of rain water into the aquifer is also a source of BHT and BHT-CHO in ground water.

Antioxidants↗
PubMed2000

A tyramine receptor gene mutation causes a defective olfactory behavior in Drosophila melanogaster.

We characterized molecular profiles of a new olfactory mutant line, honoka (hono), which was found among 500 viable P-element insertion lines screened first by 5-bromo-4-chloro-3-indrolyl-beta-D-galactopyranoside (X-gal) staining on the third segment of the antenna, and then by behavioral assays to several pure chemicals. The behavioral responses of hono mutants to repellents such as ethyl acetate (EA), benzaldehyde (BZ) and 4-methylcycrohexanol (MCH), were reduced compared with those of a control strain. The location of the P-element insertion was determined to be about 100bp) upstream of the first exon of the tyramine receptor gene. The level of 3.6kb tyramine receptor mRNA expression was reduced in hono compared with that of wild-type flies. The tyramine receptor cDNA hybridized to the chromosomal division 79C-D, the same locus as the P-element insertion point in hono, and not to 99A-B, previously reported by Arakawa et al. (1990. Neuron 2, 343-354). Electrophysiological responses to octopamine and tyramine were examined by measuring the excitatory junctional potential (EJP) amplitude from larval body-wall muscles of the hono mutant. The hono was impaired with responding to tyramine, while displaying normal response to octopamine. These results indicate that tyramine has a functional role in the Drosophila olfactory system as a neurotransmitter or a neuromodulator, and hono is the first tyramine receptor mutant. This study provides the first step toward understanding of the molecular genetics of tyramine-mediated neural functions in Drosophila.

Acetates↗
PubMed2003

Effects of olfactory function, age, and gender on trigeminally mediated sensations: a study based on the lateralization of chemosensory stimuli.

The present investigation aimed to compare trigeminal nasal function of anosmic and hyposmic patients to healthy controls. Further, we aimed to study effects of age and gender on trigeminally mediated sensations following intranasal chemosensory stimulation. Participants were 35 patients with olfactory dysfunction (n=13: functional anosmia; n=22: hyposmia; age 28-69 years, mean age 56 years). Their results were compared with 17 normosmic subjects (28-82 years, mean 52 years). To analyze effects of age and gender in healthy subjects, an additional 24 healthy subjects were included (19-27 years; mean 24 years). Olfactory function was assessed using the 'Sniffin' Sticks' test kit (butanol odor threshold, odor discrimination, odor identification). The subjects' ability to lateralize odors was investigated for benzaldehyde and eucalyptol. Patients with olfactory dysfunction had lower scores in the lateralization task than controls (P<0.001) indicating decreased trigeminal sensitivity. Among anosmic patients scores were not different in relation to different causes of olfactory dysfunction (P>0.29). There was a weak, but significant, correlation between localization of eucalyptol and duration of olfactory dysfunction (P=0.017). When investigating normosmic subjects only, no gender-related difference was apparent for lateralization scores. However, older subjects had lower scores than younger ones (P<0.01). Results of partial correlational analyses controlling for age suggested a relation between the trigeminal and the olfactory systems. In conclusion, results of the present study indicate that patients with olfactory dysfunction have lower trigeminal sensitivity compared with normosmic controls. This seems to be independent of the cause of olfactory loss. The deficit appears to improve with duration of the olfactory dysfunction, possibly indicating adaptive mechanisms. Further, the data suggest an age-related decrease of intranasal trigeminal sensitivity in healthy subjects. Analyses additionally indicate a correlation between olfactory and trigeminal sensitivity.

Adult↗
PubMedDate not supplied

Mechanism for the inhibition of aldehyde dehydrogenase by nitric oxide.

The inhibition of Saccharomyces cerevisiae aldehyde dehydrogenase (AlDH) by gaseous nitric oxide (NO) in solution and by NO generated from diethylamine nonoate was time and concentration dependent. The presence of oxygen significantly reduced the extent of inhibition by NO, indicating that NO itself rather than an oxidation product of NO such as N2O3 is the inhibitory species under physiological conditions. A cysteine residue at the active site of the enzyme was implicated in this inhibition based on the following observations: a) NAD+ and NADP+, but not reduced cofactors, significantly enhanced inhibition of AlDH by NO; b) the aldehyde substrate, benzaldehyde, blocked inhibition; and c) inhibition was accompanied by loss of free sulfhydryl groups on the enzyme. Activity of the NO-inactivated enzyme was readily restored by treatment with dithiothreitol (DTT), but not with GSH. This difference was attributed, in part, to a redox process leading to the formation of a cyclic DTT disulfide. Based on the chemistry deduced from model systems, the reaction of NO with AlDH sulfhydryls was shown to produce intramolecular disulfides and N2O. These disulfides were shown to be intrasubunit disulfides by nonreducing SDS-PAGE analysis of the NO- inhibited enzyme. Following complete inhibition of AlDH by NO, four of the eight titratable (Ellman's reagent) sulfhydryl groups of AlDH were found to be oxidized to disulfides. These results suggest that a) the sulfhydryl group of active site Cys-302 and a proximal cysteine are oxidized to form an intrasubunit disulfide by NO; b) only two of the four subunits of AlDH are catalytically active; and c) NO preferentially oxidizes sulfhydryl groups of the catalytically active subunits. A detailed mechanism for the inhibition of AlDH by NO is presented.

Aldehyde Dehydrogenase↗
PubMed2000

Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification.

Aldehyde oxidase (EC 1.2.3.1) in monkey (Macaca fascicularis) liver was characterized. Liver cytosol exhibited extremely high benzaldehyde and phthalazine oxidase activities based on aldehyde oxidase, compared with those of rabbits, rats, mice and guinea pigs. Monkey liver aldehyde oxidase showed broad substrate specificity distinct from that of the enzyme from other mammals. Purified aldehyde oxidase from monkey liver cytosol showed two major bands and two minor bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These bands were also observed in Western blotting analysis using anti-rat aldehyde oxidase. The molecular mass of the enzyme was estimated to be 130-151 kDa by SDS-PAGE, and to be about 285 kDa by HPLC gel filtration. The results suggest that isoforms of aldehyde oxidase exist in monkey livers.

Aldehyde Oxidase↗