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| glycolaldehyde |
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| CHEBI:17071 |
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| The glycolaldehyde derived from ethylene glycol. The parent of the class of glycolaldehydes. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:5474, CHEBI:14347, CHEBI:24386
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| ChemicalBook:CB51456366 |
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Molfile
XML
SDF
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more structures >>
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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js Jmol JavaScript applet jmolApplet0_object__400897421613644__ initializing getValue debug = null getValue logLevel = null getValue allowjavascript = null AppletRegistry.checkIn(jmolApplet0_object__400897421613644__) call loadScript javascripts\jsmol\core\corestate.z.js viewerOptions: { "name":"jmolApplet0_object","applet":true,"documentBase":"https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24386","platform":"J.awtjs2d.Platform","fullName":"jmolApplet0_object__400897421613644__","display":"jmolApplet0_canvas2d","signedApplet":"true","appletReadyCallback":"Jmol._readyCallback","statusListener":"[J.appletjs.Jmol.MyStatusListener object]","codeBase":"https://www.ebi.ac.uk/chebi/javascripts/jsmol/","syncId":"400897421613644","bgcolor":"#000" } (C) 2012 Jmol Development Jmol Version: 13.2.7 $Date: 2013-10-01 11:35:15 -0500 (Tue, 01 Oct 2013) $ java.vendor: j2s java.version: 0.0 os.name: j2s Access: ALL memory: 0.0/0.0 processors available: 1 useCommandThread: false appletId:jmolApplet0_object (signed) starting HoverWatcher_1 getValue emulate = null defaults = "Jmol" getValue boxbgcolor = null getValue bgcolor = #000 backgroundColor = "#000" getValue ANIMFRAMECallback = null getValue APPLETREADYCallback = Jmol._readyCallback APPLETREADYCallback = "Jmol._readyCallback" getValue ATOMMOVEDCallback = null getValue CLICKCallback = null getValue ECHOCallback = null getValue ERRORCallback = null getValue EVALCallback = null getValue HOVERCallback = null getValue LOADSTRUCTCallback = null getValue MEASURECallback = null getValue MESSAGECallback = null getValue MINIMIZATIONCallback = null getValue PICKCallback = null getValue RESIZECallback = null getValue SCRIPTCallback = null getValue SYNCCallback = null getValue STRUCTUREMODIFIEDCallback = null getValue doTranslate = null language=en_US getValue popupMenu = null getValue script = null Jmol applet jmolApplet0_object__400897421613644__ ready call loadScript javascripts\jsmol\core\corescript.z.js call loadScript javascripts\jsmol\J\script\FileLoadThread.js starting QueueThread0_2 script 1 started starting HoverWatcher_3 starting HoverWatcher_4 The Resolver thinks Mol DW3 - Ideal conformer Mrv1927 06062214053D starting HoverWatcher_5 Time for openFile(DW3 - Ideal conformer Mrv1927 06062214053D 8 7 0 0 0 0 999 V2000 -0.7050 -0.2610 -0.3520 C 0 0 0 0 0 0 0 0 0 0 0 0 0.5490 0.5530 -0.1600 C 0 0 1 0 0 0 0 0 0 0 0 0 -1.7000 0.0050 0.2780 O 0 0 0 0 0 0 0 0 0 0 0 0 1.6330 -0.3140 0.1800 O 0 0 0 0 0 0 0 0 0 0 0 0 -0.7150 -1.0800 -1.0560 H 0 0 0 0 0 0 0 0 0 0 0 0 0.7830 1.0830 -1.0830 H 0 0 0 0 0 0 0 0 0 0 0 0 0.3950 1.2740 0.6430 H 0 0 0 0 0 0 0 0 0 0 0 0 2.4730 0.1430 0.3180 H 0 0 0 0 0 0 0 0 0 0 0 0 1 3 2 0 0 0 0 1 2 1 0 0 0 0 2 4 1 0 0 0 0 1 5 1 0 0 0 0 2 6 1 0 0 0 0 2 7 1 0 0 0 0 4 8 1 0 0 0 0 M END): 14 ms reading 8 atoms ModelSet: haveSymmetry:false haveUnitcells:false haveFractionalCoord:false 1 model in this collection. Use getProperty "modelInfo" or getProperty "auxiliaryInfo" to inspect them. Default Van der Waals type for model set to Babel 8 atoms created ModelSet: not autobonding; use forceAutobond=true to force automatic bond creation Script completed Jmol script terminated
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| Glycolaldehyde is the organic compound with the formula HOCH2−CHO. It is the smallest possible molecule that contains both an aldehyde group (−CH=O) and a hydroxyl group (−OH). It is a highly reactive molecule that occurs both in the biosphere and in the interstellar medium. It is normally supplied as a white solid. Although it conforms to the general formula for carbohydrates, Cn(H2O)n, it is not generally considered to be a saccharide.
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Read full article at Wikipedia
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| InChI=1S/C2H4O2/c3-1-2-4/h1,4H,2H2 |
| WGCNASOHLSPBMP-UHFFFAOYSA-N |
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Saccharomyces cerevisiae
(NCBI:txid4932)
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Source: yeast.sf.net
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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fundamental metabolite
Any metabolite produced by all living cells.
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
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View more via ChEBI Ontology
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GLYCOALDEHYDE
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ChemIDplus
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Glycolaldehyde
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KEGG COMPOUND
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glycolaldehyde
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UniProt
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Glycolic aldehyde
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ChemIDplus
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glycollaldehyde
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NIST Chemistry WebBook
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Hydroxyacetaldehyde
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KEGG COMPOUND
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Methylol formaldehyde
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ChemIDplus
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Monomethylolformaldehyde
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ChemIDplus
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141-46-8
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CAS Registry Number
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KEGG COMPOUND
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141-46-8
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CAS Registry Number
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NIST Chemistry WebBook
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141-46-8
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CAS Registry Number
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ChemIDplus
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506029
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Reaxys Registry Number
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Reaxys
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Gu MJ, Hyon JY, Lee HW, Han EH, Kim Y, Cha YS, Ha SK (2022)
Glycolaldehyde, an Advanced Glycation End Products Precursor, Induces Apoptosis via ROS-Mediated Mitochondrial Dysfunction in Renal Mesangial Cells.
Antioxidants (Basel, Switzerland) 11, 934 [PubMed:35624799]
[show Abstract]
Glycolaldehyde (GA) is a reducing sugar and a precursor of advanced glycation end products (AGEs). The role of precursor and precursor-derived AGEs in diabetes and its complications have been actively discussed in the literature. This study aimed to elucidate the mechanism of GA-induced apoptosis in renal cells. Immunoblotting results showed that GA (100 μM) caused cytotoxicity in murine renal glomerular mesangial cells (SV40 MES 13) and induced apoptosis via major modulators, decreasing Bcl-2 and increasing Bax, cytochrome c, and cleaved caspase-3/-9 expression. GA-derived AGE accumulation and receptor for AGE (RAGE) expression increased in mesangial cells; however, cells that were cotreated with aminoguanidine (AG) showed no increase in GA-derived AGE concentration. Furthermore, reactive oxygen species (ROS) production was increased by GA, while AG inhibited AGE formation, leading to a decrease in ROS levels in mesangial cells. We evaluated apoptosis through fluorescence-activated cell sorting, and used TUNEL staining to study DNA fragmentation. Additionally, we measured ATP generation and used MitoTracker staining to access changes in mitochondrial membrane potential. This study showed that GA increased AGE concentration, RAGE expression, and excessive ROS generation, leading to renal mesangial cell damage via GA-induced apoptosis pathway caused by mitochondrial dysfunction. | Rau R, Glomb MA (2022)
Novel Pyridinium Cross-Link Structures Derived from Glycolaldehyde and Glyoxal.
Journal of agricultural and food chemistry 70, 4434-4444 [PubMed:35348319]
[show Abstract]
Short-chained α-hydroxycarbonyl compounds such as glycolaldehyde (GA) and its oxidized counterpart glyoxal (GX) are known as potent glycating agents. Here, a novel fluorescent lysine-lysine cross-link 1-(5-amino-5-carboxypentyl)-3-(5-amino-5-carboxy-pentylamino)pyridinium salt (meta-DLP) was synthesized and its structure unequivocally proven by 1H NMR, 13C-NMR attached proton test, and 2D NMR. Further characterization of chemical properties and mechanistic background was obtained in comparison to the known monovalent protein modification 2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine). Identification and quantitation in various sugar incubations with N2-t-Boc-lysine revealed a novel alternative formation pathway for both advanced glycation end products (AGEs) by the interplay of both carbonyl compounds, GA and GX, which was confirmed by isotope labeling experiments. The concentration of pyridinium AGEs was about 1000-fold lower compared to the well-established N6-carboxymethyl lysine. However, pyridinium AGEs were shown to lead to the photosensitized generation of singlet oxygen in irradiation experiments, which was verified by the detection of 3,3'-(naphthalene-1,4-diyl)-dipropionate endoperoxide. Furthermore, meta-DLP was identified in hydrolyzed potato chip proteins by collision-induced dissociation mass spectrometry after HPLC enrichment. | Klaus A, Baldensperger T, Fiedler R, Girndt M, Glomb MA (2018)
Influence of Transketolase-Catalyzed Reactions on the Formation of Glycolaldehyde and Glyoxal Specific Posttranslational Modifications under Physiological Conditions.
Journal of agricultural and food chemistry 66, 1498-1508 [PubMed:29400466]
[show Abstract]
In the present study, we investigated the role of transketolase (TK) in the modulation of glycolaldehyde driven Maillard reactions. In vitro experiments with recombinant human TK reduced glycolaldehyde and glyoxal induced carbonyl stress and thereby suppressed the formation of advanced glycation endproducts up to 70% due to the enzyme-catalyzed conversion of glycolaldehyde to erythrulose. This was further substantiated by the use of 13C-labeled compounds. For the first time, glycolaldehyde and other sugars involved in the TK reaction were quantified in vivo and compared to nondiabetic uremic patients undergoing hemodialysis. Quantitation revealed amounts of glycolaldehyde up to 2 μM and highlighted its crucial role in the formation of AGEs in vivo. In this context, a LC-MS2 method for the comprehensive detection of sedoheptulose-7-phosphate, fructose-6-phosphate, ribose-5-phosphate, erythrose-4-phosphate, erythrulose, and glycolaldehyde in whole blood, plasma, and red blood cells was established and validated based on derivatization with 1-naphthylamine and sodium cyanoborohydride. | Chikazawa M, Otaki N, Shibata T, Miyashita H, Kawai Y, Maruyama S, Toyokuni S, Kitaura Y, Matsuda T, Uchida K (2013)
Multispecificity of immunoglobulin M antibodies raised against advanced glycation end products: involvement of electronegative potential of antigens.
The Journal of biological chemistry 288, 13204-13214 [PubMed:23543734]
[show Abstract]
BackgroundAdvanced glycation end products (AGEs) can act as neoantigens to trigger immune responses.ResultsNatural IgM antibodies against AGEs recognize multiple molecules, including DNA and chemically modified proteins.ConclusionThere is a close relationship between the formation of AGEs and innate immune responses.SignificanceOur findings highlight AGEs and related modified proteins as a source of multispecific natural antibodies Advanced glycation end products (AGEs) are a heterogeneous and complex group of compounds that are formed when reducing sugars, such as dehydroascorbic acid, react in a nonenzymatic way with amino acids in proteins and other macromolecules. AGEs are prevalent in the diabetic vasculature and contribute to the development of atherosclerosis. The presence and accumulation of AGEs in many different cell types affect the extracellular and intracellular structure and function. In the present study, we studied the immune response to the dehydroascorbic acid-derived AGEs and provide multiple lines of evidence suggesting that the AGEs could be an endogenous source of innate epitopes recognized by natural IgM antibodies. Prominent IgM titers to the AGEs were detected in the sera of normal mice and were significantly accelerated by the immunization with the AGEs. Patients with systemic lupus erythematosus (SLE), a potentially fatal systemic autoimmune disease characterized by the increased production of autoantibodies, showed significantly higher serum levels of the IgM titer against the AGEs than healthy individuals. A progressive increase in the IgM response against the AGEs was also observed in the SLE-prone mice. Strikingly, a subset of monoclonal antibodies, showing a specificity toward the AGEs, prepared from normal mice immunized with the AGEs and from the SLE mice cross-reacted with the double-stranded DNA. Moreover, they also cross-reacted with several other modified proteins, including the acetylated proteins, suggesting that the multiple specificity of the antibodies might be ascribed, at least in part, to the increased electronegative potential of the proteins. These findings suggest that the protein modification by the endogenous carbonyl compounds, generating electronegative proteins, could be a source of multispecific natural antibodies. | Isobe K, Kataoka M, Ogawa J, Hasegawa J, Shimizu S (2012)
Microbial oxidases catalyzing conversion of glycolaldehyde into glyoxal.
New biotechnology 29, 177-182 [PubMed:21820089]
[show Abstract]
The present paper reviews oxidases catalyzing conversion of glycolaldehyde into glyoxal. The enzymatic oxidation of glycolaldehyde into glyoxal was first reported in alcohol oxidases (AODs) from methylotrophic yeasts such as Candida and Pichia, and glycerol oxidase (GLOD) from Aspergillus japonicus, although it had been reported that these enzymes are specific to short-chain linear aliphatic alcohols and glycerol, respectively. These enzymes continuously oxidized ethylene glycol into glyoxal via glycolaldehyde. The AODs produced by Aspergillus ochraceus and Penicillium purpurescens also oxidized glycolaldehyde. A new enzyme exhibiting oxidase activity for glycolaldehyde was reported from a newly isolated bacterium, Paenibacillus sp. AIU 311. The Paenibacillus enzyme exhibited high activity for aldehyde alcohols such as glycolaldehyde and glyceraldehyde, but not for methanol, ethanol, ethylene glycol or glycerol. The deduced amino acid sequence of the Paenibacillus AOD was similar to that of superoxide dismutases (SODs), but not to that of methylotrophic yeast AODs. Then, it was demonstrated that SODs had oxidase activity for aldehyde alcohols including glycolaldehyde. The present paper describes characteristics of glycolaldehyde oxidation by those enzymes produced by different microorganisms. | Jayakody LN, Hayashi N, Kitagaki H (2011)
Identification of glycolaldehyde as the key inhibitor of bioethanol fermentation by yeast and genome-wide analysis of its toxicity.
Biotechnology letters 33, 285-292 [PubMed:20960220]
[show Abstract]
Degradation of lignocellulose with pressurised hot water is an efficient method of bioethanol production. However, the resultant solution inhibits ethanol fermentation by Saccharomyces cerevisiae. Here, we first report that glycolaldehyde, which is formed when lignocellulose is treated with pressurised hot water, inhibits ethanol fermentation. The final concentration of glycolaldehyde formed by the treatment of lignocellulose with pressurised hot water ranges from 1 to 24 M, and 1-10 mM glycolaldehyde was sufficient to inhibit fermentation. This result indicates that glycolaldehyde is one of the main substances responsible for inhibiting fermentation after pressurised hot water degradation of lignocellulose. Genome-wide screening of S. cerevisiae revealed that genes encoding alcohol dehydrogenase, methylglyoxal reductase, polysomes, and the ubiquitin ligase complex are required for glycolaldehyde tolerance. These novel findings will provide new perspectives on breeding yeast for bioethanol production from biomass treated with pressurised hot water. | Cui G, Fang W (2011)
Mechanistic photodissociation of glycolaldehyde: insights from ab initio and RRKM calculations.
Chemphyschem : a European journal of chemical physics and physical chemistry 12, 1351-1357 [PubMed:21472960]
[show Abstract]
Herein we report a theoretical study on mechanistic photodissociation of glycolaldehyde, HOCH(2) CHO. Equilibrium structures, transition states, and intersection structures for the α-C-C and -C-H bond fissions and the β-C-O bond fission in the excited states are determined by the complete active space self-consistent field (CASSCF) method. Based on the CASSCF optimized structures, the potential energy profiles for the dissociations are refined by performing single-point calculations using the multi-state multi-reference CASSCF second order perturbation (MS-MR-CASPT2) method. With a low excitation energy of 280-340 nm, the T(1) α-C-C and β-C-O bond fissions following intersystem crossing from the S(1) state are the predominant and comparable channels, whereas the α-C-H bond fissions both in the S(1) and in the T(1) states are nearly prohibited due to the relevant high barriers. The rate constants for the T(1) α-C-C and β-C-O bond fissions are also calculated by RRKM theory. Furthermore, the S(0) reactions can occur as a consequence of intersystem crossing via T(1)/S(0) intersection points resulting from the T(1) C-C and C-O bond cleavages. This photodissociation mechanism is consistent with recent experimental studies. | Lorenzi R, Andrades ME, Bortolin RC, Nagai R, Dal-Pizzol F, Moreira JC (2011)
Oxidative damage in the liver of rats treated with glycolaldehyde.
International journal of toxicology 30, 253-258 [PubMed:21378371]
[show Abstract]
Liver diseases are often associated with hyperglycemia, inflammation, and oxidative stress. These conditions, commonly associated with diabetes mellitus and obesity, facilitate the formation of advanced glycation end products (AGEs). These products are known to impair protein function and promote inflammation. Accumulation of AGEs such as N(ε)-(carboxymethyl)lysine (CML) is related to chronic liver diseases and their severity. Although several reports suggest a crucial role of AGEs in liver failure, there is little investigation on the direct effects of reducing sugars, precursors of AGEs, and on the onset and progression of liver failure. In this work, we investigate the effects of intravenously administrated glycolaldehyde (GA), a short-chain aldehyde, on oxidative parameters in the liver of Wistar rats. Animals received a single injection of GA (10, 50, or 100 mg/kg) and were sacrificed after 6, 12, or 24 hours. Levels of protein carbonyl, lipid peroxidation, and reduced thiol were quantified. The activities of catalase, superoxide dismutase, and glyoxalase I were also assessed. The amount of CML was quantified with specific antibody. There was an increase in oxidative stress markers in the liver of GA-treated rats. Glycolaldehyde induced a decrease in the activities of all enzymes assayed. Also, all tested doses led to an increase in CML content. Our data suggest that GA might play an important role in liver diseases through the impairment of antioxidant defenses and generation of AGEs. |
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