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Journal articles on the topic 'Aldehyde Dehydrogenase Inhibition'

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Published: 2 June 2025

Last updated: 31 July 2025

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1

Averill-Bates, Diana A., Enzo Agostinelli, Ewa Przybytkowski, and Bruno Mondovi. "Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells." Biochemistry and Cell Biology 72, no. 1-2 (1994): 36–42. http://dx.doi.org/10.1139/o94-006.

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Bovine serum amine oxidase (EC 1.4.3.6) catalyses the oxidative deamination of polyamines giving rise to the corresponding aldehydes, ammonia, and hydrogen peroxide. It has been suggested that the dialdehyde produced during the oxidation of spermine subsequently undergoes spontaneous β-elimination to form acrolein. Oxidation of the aldehydes by aldehyde dehydrogenase (EC 1.2.1.5) thus eliminates these reactive species and prevents the formation of acrolein. This work studies the role of each of the oxidation products of spermine in cytotoxicity induced by purified bovine serum amine oxidase. T

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2

Chen, Chao, Jeong Chan Joo, Greg Brown, et al. "Structure-Based Mutational Studies of Substrate Inhibition of Betaine Aldehyde Dehydrogenase BetB from Staphylococcus aureus." Applied and Environmental Microbiology 80, no. 13 (2014): 3992–4002. http://dx.doi.org/10.1128/aem.00215-14.

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ABSTRACTInhibition of enzyme activity by high concentrations of substrate and/or cofactor is a general phenomenon demonstrated in many enzymes, including aldehyde dehydrogenases. Here we show that the uncharacterized protein BetB (SA2613) fromStaphylococcus aureusis a highly specific betaine aldehyde dehydrogenase, which exhibits substrate inhibition at concentrations of betaine aldehyde as low as 0.15 mM. In contrast, the aldehyde dehydrogenase YdcW fromEscherichia coli, which is also active against betaine aldehyde, shows no inhibition by this substrate. Using the crystal structures of BetB

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3

MODIG, Tobias, Gunnar LIDÉN, and Mohammad J. TAHERZADEH. "Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase." Biochemical Journal 363, no. 3 (2002): 769–76. http://dx.doi.org/10.1042/bj3630769.

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The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity decreased by less than 20% at the same concentration. Furfural inhibition of ADH and AlDH activities could be described well by a competitive inhibition model, whereas the inhibition of PDH was best described as non-competitive. The estimated Km value of

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4

Karamanakos, Petros N., Periklis Pappas, Vassiliki A. Boumba, et al. "Pharmaceutical Agents Known to Produce Disulfiram-Like Reaction: Effects on Hepatic Ethanol Metabolism and Brain Monoamines." International Journal of Toxicology 26, no. 5 (2007): 423–32. http://dx.doi.org/10.1080/10915810701583010.

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Several pharmaceutical agents produce ethanol intolerance, which is often depicted as disulfiram-like reaction. As in the case with disulfiram, the underlying mechanism is believed to be the accumulation of acetaldehyde in the blood, due to inhibition of the hepatic aldehyde dehydrogenases. In the present study, chloramphenicol, furazolidone, metronidazole, and quinacrine, which are reported to produce a disulfiram-like reaction, as well as disulfiram, were administered to Wistar rats and the hepatic activities of alcohol and aldehyde dehydrogenases (1A1 and 2) were determined. The expression

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5

Panoutsopoulos, Georgios I., and Christine Beedham. "Enzymatic oxidation of phthalazine with guinea pig liver aldehyde oxidase and liver slices: inhibition by isovanillin." Acta Biochimica Polonica 51, no. 4 (2004): 943–51. https://doi.org/10.18388/abp.2004_3527.

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The enzymes aldehyde oxidase and xanthine oxidase catalyze the oxidation of a wide range of N-heterocycles and aldehydes. These enzymes are widely known for their role in the metabolism of N-heterocyclic xenobiotics where they provide a protective barrier by aiding in the detoxification of ingested nitrogen-containing heterocycles. Isovanillin has been shown to inhibit the metabolism of aromatic aldehydes by aldehyde oxidase, but its inhibition towards the heterocyclic compounds has not been studied. The present investigation examines the oxidation of phthalazine in the absence and in the pres

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6

Dicker, E., and A. I. Cederbaum. "Inhibition of the low-Km mitochondrial aldehyde dehydrogenase by diethyl maleate and phorone in vivo and in vitro Implications for formaldehyde metabolism." Biochemical Journal 240, no. 3 (1986): 821–27. http://dx.doi.org/10.1042/bj2400821.

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Formaldehyde can be oxidized primarily by two different enzymes, the low-Km mitochondrial aldehyde dehydrogenase and the cytosolic GSH-dependent formaldehyde dehydrogenase. Experiments were carried out to evaluate the effects of diethyl maleate or phorone, agents that deplete GSH from the liver, on the oxidation of formaldehyde. The addition of diethyl maleate or phorone to intact mitochondria or to disrupted mitochondrial fractions produced inhibition of formaldehyde oxidation. The kinetics of inhibition of the low-Km mitochondrial aldehyde dehydrogenase were mixed. Mitochondria isolated from

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7

Paulová, Hana, Jan Kovář, Jiří Plocek, and Jiří Slavík. "Inhibition of aldehyde reductase I by some isoquinoline alkaloids." Collection of Czechoslovak Chemical Communications 52, no. 9 (1987): 2338–46. http://dx.doi.org/10.1135/cccc19872338.

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Aldehyde reductase I has been found to be inhibited by certain isoquinoline alkaloids (protoberberines, protopines, benzylisoquinolines, benzyltetrahydroisoquinolines, phthalideisoquinolines, pavinanes) and narceine imide. The sensitivity of this enzyme to the compounds tested was compared with that of alcohol dehydrogenase and/or aldehyde reductase II to them; alcohol dehydrogenase proved more selective in binding the alkaloids. The kinetics of the inhibitory action of berberine and other results suggest that the binding site of aldehyde reductase I for alkaloids is relatively large, has a hy

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8

Yusuf, Rushdia Zareen, Borja Saez, Azeem Sharda, et al. "Aldehyde dehydrogenase 3a2 protects AML cells from oxidative death and the synthetic lethality of ferroptosis inducers." Blood 136, no. 11 (2020): 1303–16. http://dx.doi.org/10.1182/blood.2019001808.

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Abstract Metabolic alterations in cancer represent convergent effects of oncogenic mutations. We hypothesized that a metabolism-restricted genetic screen, comparing normal primary mouse hematopoietic cells and their malignant counterparts in an ex vivo system mimicking the bone marrow microenvironment, would define distinctive vulnerabilities in acute myeloid leukemia (AML). Leukemic cells, but not their normal myeloid counterparts, depended on the aldehyde dehydrogenase 3a2 (Aldh3a2) enzyme that oxidizes long-chain aliphatic aldehydes to prevent cellular oxidative damage. Aldehydes are by-pro

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9

Keller, Markus A., Katrin Watschinger, Georg Golderer, Gabriele Werner-Felmayer, and Ernst R. Werner. "Fatty aldehyde dehydrogenase, the enzyme downstream of tetrahydrobiopterin-dependent alkylglycerol monooxygenase." Pteridines 24, no. 1 (2013): 105–9. http://dx.doi.org/10.1515/pterid-2013-0004.

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AbstractThe tetrahydrobiopterin-dependent degradation of ether lipids by alkylglycerol monooxygenase (AGMO) produces fatty aldehydes, which are toxic to cells. Therefore, it is of great physiological importance that these harmful compounds are converted into their corresponding, less toxic fatty acids by fatty aldehyde dehydrogenase (FALDH). Dysfunction of this enzyme causes Sjögren-Larsson syndrome. This severe inherited disorder is accompanied by symptoms such as ichthyosis, mental retardation and spasticity. Surprisingly, fatty alcohols and not fatty aldehydes were found to accumulate in fi

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10

VELASCO-GARCÍA, Roberto, Lilian GONZÁLEZ-SEGURA, and Rosario A. MUÑOZ-CLARES. "Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa." Biochemical Journal 352, no. 3 (2000): 675–83. http://dx.doi.org/10.1042/bj3520675.

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Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)+ to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD+- and NADP+-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)+ and for product and dead-end inhibition e

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11

Laskar, Amaj Ahmed, Masood Alam Khan, Sumbul Ahmad, Amiruddin Hashmi, and Hina Younus. "Citral Inhibition of Human Salivary Aldehyde Dehydrogenase." Cell Biochemistry and Biophysics 78, no. 1 (2019): 31–42. http://dx.doi.org/10.1007/s12013-019-00891-4.

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12

MODIG, Tobias, Gunnar LIDÉN, and Mohammad J. TAHERZADEH. "Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase." Biochemical Journal 363, no. 3 (2002): 769. http://dx.doi.org/10.1042/0264-6021:3630769.

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13

Heinstra, P. W. H., B. W. Geer, D. Seykens, and M. Langevin. "The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae." Biochemical Journal 259, no. 3 (1989): 791–97. http://dx.doi.org/10.1042/bj2590791.

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Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme. The larval fat body probably was the ma

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14

Кислова, О. В. "ВПЛИВ ЗАМІЩЕННОГО НІКОТИНАМІДУ ТА ЙОГО МОЖЛИВИХ МЕТАБОЛІТІВ НА АКТИВНІСТЬ ФЕРМЕНТІВ ОБМІНУ ЕТАНОЛУ". Bulletin of the Kyiv National University of Technologies and Design. Technical Science Series 144, № 2 (2020): 98–104. http://dx.doi.org/10.30857/1813-6796.2020.2.10.

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To study the influence of N-phenyl-N-(1-cyclopropylethyl)nicotinamide and its possible metabolites: hydrochlorides of N-(1-cyclopropylethyl)amine and N-phenyl-N-(1-cyclopropylethyl)amine - on the activity of main ethanol oxidation enzymes in vitro and kinetic nature of their interaction. The studies were carried out using alcohol dehydrogenase and aldehyde dehydrogenase of rat liver subcellular fractions, which were obtained by differential centrifugation. The enzyme activity was determined spectrophotometrically. The kinetic nature of alcohol dehydrogenase and isozyme form of aldehyde dehydro

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15

Lipsky, James J., Maryann L. Shen, and Stephen Naylor. "In vivo inhibition of aldehyde dehydrogenase by disulfiram." Chemico-Biological Interactions 130-132 (January 2001): 93–102. http://dx.doi.org/10.1016/s0009-2797(00)00225-8.

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16

Schräder, Thomas, Grit Zarnt, and Jan R. Andreesen. "NAD(P)-Dependent Aldehyde Dehydrogenases Induced during Growth of Ralstonia eutropha Strain Bo on Tetrahydrofurfuryl Alcohol." Journal of Bacteriology 183, no. 24 (2001): 7408–11. http://dx.doi.org/10.1128/jb.183.24.7408-7411.2001.

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ABSTRACT Different aldehyde dehydrogenases (AlDHs) were formed during growth of Ralstonia eutropha Bo on tetrahydrofurfuryl alcohol (THFA). One of these enzymes, AlDH 4, was purified and characterized as a homodimer containing no prosthetic groups, showing a strong substrate inhibition, and having an N-terminal sequence similar to those of various NAD(P)-dependent AlDHs. The conversion rate of THFA by the quinohemoprotein THFA dehydrogenase was increased by AlDH 4.

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17

Boumya, Sara, Silvia Fallarini, Sonia Siragusa, et al. "A Selective ALDH1A3 Inhibitor Impairs Mesothelioma 3-D Multicellular Spheroid Growth and Neutrophil Recruitment." International Journal of Molecular Sciences 24, no. 7 (2023): 6689. http://dx.doi.org/10.3390/ijms24076689.

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Aldehyde dehydrogenase 1A3 (ALDH1A3), one of the three members of the aldehyde dehydrogenase 1A subfamily, has been associated with increased progression and drug resistance in various types of solid tumours. Recently, it has been reported that high ALDH1A3 expression is prognostic of poor survival in patients with malignant pleural mesothelioma (MPM), an asbestos-associated chemoresistant cancer. We treated MPM cells, cultured as multicellular spheroids, with NR6, a potent and highly selective ALDH1A3 inhibitor. Here we report that NR6 treatment caused the accumulation of toxic aldehydes, ind

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18

Carper, W. R., R. C. Dorey, and J. H. Beber. "Inhibitory effect of disulfiram (Antabuse) on alcohol dehydrogenase activity." Clinical Chemistry 33, no. 10 (1987): 1906–8. http://dx.doi.org/10.1093/clinchem/33.10.1906.

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Abstract We investigated the effect of disulfiram (Antabuse) on the activity of alcohol dehydrogenase (EC 1.1.1.1) in vitro. We observed a time-dependent inhibition of this dehydrogenase by disulfiram and diethyldithiocarbamate similar to that obtained for aldehyde dehydrogenase (EC 1.2.1.3). These results suggest a possible explanation for various side effects observed in the clinical use of Antabuse.

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19

Halavaty, Andrei S., Rebecca L. Rich, Chao Chen, et al. "Structural and functional analysis of betaine aldehyde dehydrogenase fromStaphylococcus aureus." Acta Crystallographica Section D Biological Crystallography 71, no. 5 (2015): 1159–75. http://dx.doi.org/10.1107/s1399004715004228.

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When exposed to high osmolarity, methicillin-resistantStaphylococcus aureus(MRSA) restores its growth and establishes a new steady state by accumulating the osmoprotectant metabolite betaine. Effective osmoregulation has also been implicated in the acquirement of a profound antibiotic resistance by MRSA. Betaine can be obtained from the bacterial habitat or produced intracellularly from cholineviathe toxic betaine aldehyde (BA) employing the choline dehydrogenase and betaine aldehyde dehydrogenase (BADH) enzymes. Here, it is shown that the putative betaine aldehyde dehydrogenase SACOL2628 from

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20

Kimble-Hill, Ann C., Hina Younus, Samy Meroueh, and Thomas D. Hurley. "Structure Based Inhibition of Mitochondrial Aldehyde Dehydrogenase (ALDH2) Activity." Biophysical Journal 100, no. 3 (2011): 215a. http://dx.doi.org/10.1016/j.bpj.2010.12.1387.

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21

Dastidar, Debabrata G., Amlan Das, Satabdi Datta, et al. "Paclitaxel-encapsulated core–shell nanoparticle of cetyl alcohol for active targeted delivery through oral route." Nanomedicine 14, no. 16 (2019): 2121–50. http://dx.doi.org/10.2217/nnm-2018-0419.

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Aim: Paclitaxel (PTX) has no clinically available oral formulations. Cetyl alcohol is metabolized by alcohol dehydrogenase and aldehyde dehydrogenase that are overexpressed in cancer cells. So, PTX-encapsulated core–shell nanoparticle of cetyl alcohol (PaxSLN) could target the cancer cells through oral route. Materials & methods: PaxSLN was synthesized using microemulsion template. Efficiency of PaxSLN was evaluated by ALDEFLUOR™, multicellular tumor spheroid formation inhibition assays and CT26 colorectal carcinoma animal model. Pharmacokinetics and biodistribution studies were done in Sp

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22

Pan, Guodong, Mandar Deshpande, Rajarajan A. Thandavarayan, and Suresh Selvaraj Palaniyandi. "ALDH2 Inhibition Potentiates High Glucose Stress-Induced Injury in Cultured Cardiomyocytes." Journal of Diabetes Research 2016 (2016): 1–8. http://dx.doi.org/10.1155/2016/1390861.

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Aldehyde dehydrogenase (ALDH) gene superfamily consists of 19 isozymes. They are present in various organs and involved in metabolizing aldehydes that are biologically generated. For instance, ALDH2, a cardiac mitochondrial ALDH isozyme, is known to detoxify 4-hydroxy-2-nonenal, a reactive aldehyde produced upon lipid peroxidation in diabetic conditions. We hypothesized that inhibition of ALDH leads to the accumulation of unmetabolized 4HNE and consequently exacerbates injury in cells subjected to high glucose stress. H9C2 cardiomyocyte cell lines were pretreated with 10 μM disulfiram (DSF), a

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23

Rosas-Rodríguez, Jesús A., Ciria G. Figueroa-Soto, and Elisa M. Valenzuela-Soto. "Inhibition of porcine kidney betaine aldehyde dehydrogenase by hydrogen peroxide." Redox Report 15, no. 6 (2010): 282–87. http://dx.doi.org/10.1179/135100010x12826446921941.

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24

Fitzmaurice, A. G., S. L. Rhodes, A. Lulla, et al. "Aldehyde dehydrogenase inhibition as a pathogenic mechanism in Parkinson disease." Proceedings of the National Academy of Sciences 110, no. 2 (2012): 636–41. http://dx.doi.org/10.1073/pnas.1220399110.

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25

DeMaster, Eugene G., Beth Redfern, Barry J. Quast, Todd Dahlseid, and Herbert T. Nagasawa. "Mechanism for the inhibition of aldehyde dehydrogenase by nitric oxide." Alcohol 14, no. 2 (1997): 181–89. http://dx.doi.org/10.1016/s0741-8329(96)00142-5.

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26

Russo, James E., Denise Hauquitz, and John Hilton. "Inhibition of mouse cytosolic aldehyde dehydrogenase by 4-(diethylamino)benzaldehyde." Biochemical Pharmacology 37, no. 8 (1988): 1639–42. http://dx.doi.org/10.1016/0006-2952(88)90030-5.

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27

Moon, Kwan-Hoon, Bong-Jo Kim, and Byoung J. Song. "Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediatedS-nitrosylation." FEBS Letters 579, no. 27 (2005): 6115–20. http://dx.doi.org/10.1016/j.febslet.2005.09.082.

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28

Maninang, John S., Shin Okazaki, and Yoshiharu Fujii. "Cyanamide Phytotoxicity in Soybean (Glycine max) Seedlings involves Aldehyde Dehydrogenase Inhibition and Oxidative Stress." Natural Product Communications 10, no. 5 (2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000511.

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The phytotoxic effect of the allelochemical cyanamide has been well-documented yet the underlying mechanism for this phenomenon has not been fully characterized. Cognizant of the putative inhibitory effect of cyanamide on aldehyde dehydrogenases (ALDHs), we hereby show that the capacity of mitochondrial preparations from cyanamide-treated soybean seedlings to oxidize acetaldehyde and succinic-semialdehyde was dose-dependently reduced to at most 55% and 70%, respectively. Cyanamide-treated plants exhibited oxidative stress (i.e. increased lipid peroxidation and H2O2 accumulation) that was exace

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29

Jung, Jin Hwa, and Sun Bok Lee. "Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase." Biochemical Journal 397, no. 1 (2006): 131–38. http://dx.doi.org/10.1042/bj20051763.

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Thermoacidophilic archaea such as Thermoplasma acidophilum and Sulfolobus solfataricus are known to metabolize D-glucose via the nED (non-phosphorylated Entner–Doudoroff) pathway. In the present study, we identified and characterized a glyceraldehyde dehydrogenase involved in the downstream portion of the nED pathway. This glyceraldehyde dehydrogenase was purified from T. acidophilum cell extracts by sequential chromatography on DEAE-Sepharose, Q-Sepharose, Phenyl-Sepharose and Affi-Gel Blue columns. SDS/PAGE of the purified enzyme showed a molecular mass of approx. 53 kDa, whereas the molecul

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30

Davidson, V. L., M. E. Graichen, and L. H. Jones. "Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase." Biochemical Journal 308, no. 2 (1995): 487–92. http://dx.doi.org/10.1042/bj3080487.

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Allylamine did not serve as an efficient substrate for methylamine dehydrogenase (EC 1.4.99.3) in a steady-state assay of activity and appeared to act as a competitive inhibitor of methylamine oxidation by methylamine dehydrogenase. Transient kinetic studies, however, revealed that allylamine rapidly reduced the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase. The rate of TTQ reduction by allylamine was 322 s-1, slightly faster than the rate of reduction by methylamine. These data were explained by a kinetic mechanism in which allylamine and methylamine are alternative

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31

Henehan, G. T. M., and K. F. Tipton. "Steady-state kinetic analysis of aldehyde dehydrogenase from human erythrocytes." Biochemical Journal 287, no. 1 (1992): 145–50. http://dx.doi.org/10.1042/bj2870145.

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The steady-state kinetics of purified cytoplasmic aldehyde dehydrogenase (EC 1.2.1.3) from human erythrocytes have been studied at 37 degrees C. Previous studies of the enzyme from several mammalian sources, which used a lower assay temperature, have been difficult to interpret because of the substrate activation by acetaldehyde which led to complex kinetic behaviour. At 37 degrees C the initial-rate data do not depart significantly from Michaelis-Menten kinetics. Studies of the variation of initial rates as a function of the concentrations of both substrates and studies of the inhibition by N

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32

Vojtěchová, Martina, Rogelio Rodrı́guez-Sotres, Elisa M. Valenzuela-Soto, and Rosario A. Muñoz-Clares. "Substrate inhibition by betaine aldehyde of betaine aldehyde dehydrogenase from leaves of Amaranthus hypochondriacus L." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1341, no. 1 (1997): 49–57. http://dx.doi.org/10.1016/s0167-4838(97)00059-9.

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33

Clemens, Dahn L., Dean J. Tuma, and Carol A. Casey. "Cyanamide Potentiates the Ethanol-Induced Impairment of Receptor-Mediated Endocytosis in a Recombinant Hepatic Cell Line Expressing Alcohol Dehydrogenase Activity." International Journal of Hepatology 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/954157.

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Ethanol administration has been shown to alter receptor-mediated endocytosis in the liver. We have developed a recombinant hepatic cell line stably transfected with murine alcohol dehydrogenase cDNA to serve as anin vitromodel to investigate these ethanol-induced impairments. In the present study, transfected cells were maintained in the absence or presence of 25 mM ethanol for 7 days, and alterations in endocytosis by the asialoglycoprotein receptor were determined. The role of acetaldehyde in this dysfunction was also examined by inclusion of the aldehyde dehydrogenase inhibitor, cyanamide.

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34

Kitson, T. M. "Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase." Biochemical Journal 257, no. 2 (1989): 573–78. http://dx.doi.org/10.1042/bj2570573.

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The effects of modifiers (NAD+, NADH, propionaldehyde, chloral hydrate, diethylstilboestrol and p-nitrobenzaldehyde) on the hydrolysis of p-nitrophenyl (PNP) pivalate (PNP trimethylacetate) catalysed by cytoplasmic aldehyde dehydrogenase are reported. In each case a different inhibition pattern is obtained to that observed when the substrate is PNP acetate; for example, propionaldehyde and chloral hydrate competitively inhibit the hydrolysis of PNP acetate, but are mixed inhibitors with PNP pivalate. The kinetic results can be rationalized in terms of different rate-determining steps: acylatio

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35

Winberg, J. O., and J. S. McKinley-McKee. "Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies." Biochemical Journal 301, no. 3 (1994): 901–9. http://dx.doi.org/10.1042/bj3010901.

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The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as the leading substrate, to give two interconverting ternary complexes. The second ternary complex broke down with release of products in an obligatory order, with the aldehyde/ketone leaving first. Both

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36

Rahman, Farhana Babli, and Kiyoshi Yamauchi. "Uncompetitive Inhibition of Xenopus laevis Aldehyde Dehydrogenase 1A1 by Divalent Cations." Zoological Science 23, no. 3 (2006): 239–44. http://dx.doi.org/10.2108/zsj.23.239.

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37

Lipsky, James J., Maryann L. Shen, and Stephen Naylor. "Overview — In vitro inhibition of aldehyde dehydrogenase by disulfiram and metabolites." Chemico-Biological Interactions 130-132 (January 2001): 81–91. http://dx.doi.org/10.1016/s0009-2797(00)00224-6.

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38

Hart, Bruch W., and Morris D. Faiman. "Inhibition of rat liver low Km aldehyde dehydrogenase by thiocarbamate herbicides." Biochemical Pharmacology 49, no. 2 (1995): 157–63. http://dx.doi.org/10.1016/s0006-2952(94)00491-9.

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39

Sheikh, Saifuddin, and Henry Weiner. "Allosteric inhibition of human liver aldehyde dehydrogenase by the isoflavone prunetin." Biochemical Pharmacology 53, no. 4 (1997): 471–78. http://dx.doi.org/10.1016/s0006-2952(96)00837-4.

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40

Helander, Anders, Catharina Löwenmo, Tina Wikström, and Margareta Curvall. "Inhibition of human blood aldehyde dehydrogenase activity by cigarette-smoke condensate." Life Sciences 49, no. 25 (1991): 1901–5. http://dx.doi.org/10.1016/0024-3205(91)90291-i.

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41

Towell, John F., and Richard I. H. Wang. "Hydrogen peroxide-induced glutathione depletion and aldehyde dehydrogenase inhibition in erythrocytes." Biochemical Pharmacology 36, no. 13 (1987): 2087–93. http://dx.doi.org/10.1016/0006-2952(87)90135-3.

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42

Kikonyogo, Alexandra, Darryl P. Abriola, Marek Dryjanski, and Regina Pietruszko. "Mechanism of inhibition of aldehyde dehydrogenase by citral, a retinoid antagonist." European Journal of Biochemistry 262, no. 3 (1999): 704–12. http://dx.doi.org/10.1046/j.1432-1327.1999.00415.x.

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Johnston, C., J. B. Saunders, A. H. Barnett, B. R. Ricciardi, D. A. Hopkinson, and D. A. Pyke. "Chlorpropamide–alcohol flush reaction and isoenzyme profiles of alcohol dehydrogenase and aldehyde dehydrogenase." Clinical Science 71, no. 5 (1986): 513–17. http://dx.doi.org/10.1042/cs0710513.

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1. To investigate the enzymatic basis of the chlorpropamide–alcohol flush reaction (CPAF) we compared the isoenzyme profiles of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from liver biopsies, and of ALDH alone from erythrocytes and leucocytes, in CPAF-positive and CPAF-negative subjects. 2. No differences were seen in ADH or ALDH phenotypes, or in the relative activities of the isoenzymes, between the two groups before chlorpropamide was given; in particular, no subjects showed the ‘null’ ALDH phenotype that is associated with the alcohol flush reaction in oriental subjects.

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Bareiss, Petra M., Tanja N. Fehm, Anna Fischer, et al. "Aldehyde dehydrogenase activity in serous ovarian carcinoma." Journal of Clinical Oncology 30, no. 15_suppl (2012): e15577-e15577. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e15577.

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e15577 Background: Only specific subpopulations of tumor cells, so called cancer stem cells (CSC) may initiate and maintain tumors. The phenotype and molecular properties of ovarian CSC remain elusive. Aldehyde dehydrogenase (ALDH) activity characterizes (cancer) stem cells in different tissues and has been associated with ovarian CSC (Silva et al, 2011; Kryczek et al, 2012). Contradictory results have been reported on ALDH1 expression and prognosis in ovarian carcinoma. In this study, we explore the role of ALDH in serous ovarian carcinoma (SOC). Methods: Aldefluor-staining was used to assess

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Locquet, Marie-Anaïs, Anne-Lise Dechaume, Paul Berchard, et al. "Aldehyde Dehydrogenase, a Therapeutic Target in Chordoma: Analysis in 3D Cellular Models." Cells 10, no. 2 (2021): 399. http://dx.doi.org/10.3390/cells10020399.

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Chordomas are rare, slow-growing tumors of the axial skeleton. These tumors are locally aggressive and refractory to conventional therapies. Radical surgery and radiation remain the first-line treatments. Despite these aggressive treatments, chordomas often recur and second-line treatment options are limited. The mechanisms underlying chordoma radioresistance remain unknown, although several radioresistant cancer cells have been shown to respond favorably to aldehyde dehydrogenase (ALDH) inhibition. The study of chordoma has been delayed by small patient cohorts and few available models due to

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Page, R. A., K. E. Kitson, and M. J. Hardman. "The importance of alcohol dehydrogenase in regulation of ethanol metabolism in rat liver cells." Biochemical Journal 278, no. 3 (1991): 659–65. http://dx.doi.org/10.1042/bj2780659.

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We used titration with the inhibitors tetramethylene sulphoxide and isobutyramide to assess quantitatively the importance of alcohol dehydrogenase in regulation of ethanol oxidation in rat hepatocytes. In hepatocytes isolated from starved rats the apparent Flux Control Coefficient (calculated assuming a single-substrate irreversible reaction with non-competitive inhibition) of alcohol dehydrogenase is 0.3-0.5. Adjustment of this coefficient to allow for alcohol dehydrogenase being a two-substrate reversible enzyme increases the value by 1.3-1.4-fold. The final value of the Flux Control Coeffic

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K, Manasa, and Chitra V. "Phytoconstituents in the Management of Pesticide Induced Parkinson’s Disease- A Review." Biomedical & Pharmacology Journal 12, no. 3 (2019): 1417–24. http://dx.doi.org/10.13005/bpj/1770.

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Recent studies have suggested that environmental factors have a crucial role in triggering and/ or propagating the pathological changes in Parkinson’s disease (PD). Although many studies have been and being performed by utilizing MPTP like chemicals to study the effectiveness of new extracts and compounds in PD, a little focus was made on the role of pesticides. Since agricultural fields account for 37.7% of land area worldwide and the use of pesticides is an important risk factor in neurodegeneration, there is a crucial need to focus on the association between pesticides and PD. Benomyl, a be

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Kang, Joon Hee, Seon-Hyeong Lee, Jae-Seon Lee, et al. "Aldehyde dehydrogenase inhibition combined with phenformin treatment reversed NSCLC through ATP depletion." Oncotarget 7, no. 31 (2016): 49397–410. http://dx.doi.org/10.18632/oncotarget.10354.

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Skrott, Zdenek, Dusana Majera, Jan Gursky, et al. "Disulfiram’s anti-cancer activity reflects targeting NPL4, not inhibition of aldehyde dehydrogenase." Oncogene 38, no. 40 (2019): 6711–22. http://dx.doi.org/10.1038/s41388-019-0915-2.

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Serambeque, Beatriz, Catarina Mestre, Gabriela Correia-Barros, et al. "Influence of Aldehyde Dehydrogenase Inhibition on Stemness of Endometrial Cancer Stem Cells." Cancers 16, no. 11 (2024): 2031. http://dx.doi.org/10.3390/cancers16112031.

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Endometrial cancer is one of the most common gynaecological malignancies. Although often diagnosed at an early stage, there is a subset of patients with recurrent and metastatic disease for whom current treatments are not effective. Cancer stem cells (CSCs) play a pivotal role in triggering tumorigenesis, disease progression, recurrence, and metastasis, as high aldehyde dehydrogenase (ALDH) activity is associated with invasiveness and chemotherapy resistance. Therefore, this study aimed to evaluate the effects of ALDH inhibition in endometrial CSCs. ECC-1 and RL95-2 cells were submitted to a s

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