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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__4712807685559897__ initializing getValue debug = null getValue logLevel = null getValue allowjavascript = null AppletRegistry.checkIn(jmolApplet0_object__4712807685559897__) 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:16108","platform":"J.awtjs2d.Platform","fullName":"jmolApplet0_object__4712807685559897__","display":"jmolApplet0_canvas2d","signedApplet":"true","appletReadyCallback":"Jmol._readyCallback","statusListener":"[J.appletjs.Jmol.MyStatusListener object]","codeBase":"https://www.ebi.ac.uk/chebi/javascripts/jsmol/","syncId":"4712807685559897","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__4712807685559897__ 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 13P - Ideal conformer Mrv1927 06162116393D starting HoverWatcher_5 Time for openFile(13P - Ideal conformer Mrv1927 06162116393D 17 16 0 0 0 0 999 V2000 0.0280 -0.0400 -1.8640 P 0 0 2 0 0 5 0 0 0 0 0 0 0.7510 -1.3230 -2.0130 O 0 0 0 0 0 0 0 0 0 0 0 0 -1.1250 0.0570 -2.9830 O 0 0 0 0 0 0 0 0 0 0 0 0 1.0600 1.1810 -2.0480 O 0 0 0 0 0 0 0 0 0 0 0 0 -0.6360 0.0330 -0.4000 O 0 0 0 0 0 0 0 0 0 0 0 0 0.4310 -0.0580 0.5430 C 0 0 2 0 0 0 0 0 0 0 0 0 -0.1260 0.0050 1.9420 C 0 0 0 0 0 0 0 0 0 0 0 0 -1.3160 0.1180 2.1120 O 0 0 0 0 0 0 0 0 0 0 0 0 0.8000 -0.0710 3.1270 C 0 0 2 0 0 0 0 0 0 0 0 0 0.0380 0.0100 4.3340 O 0 0 0 0 0 0 0 0 0 0 0 0 -0.6850 0.0090 -3.8430 H 0 0 0 0 0 0 0 0 0 0 0 0 0.5490 1.9960 -1.9440 H 0 0 0 0 0 0 0 0 0 0 0 0 1.1240 0.7690 0.3900 H 0 0 0 0 0 0 0 0 0 0 0 0 0.9580 -1.0020 0.4050 H 0 0 0 0 0 0 0 0 0 0 0 0 1.5090 0.7560 3.0890 H 0 0 0 0 0 0 0 0 0 0 0 0 1.3430 -1.0160 3.1040 H 0 0 0 0 0 0 0 0 0 0 0 0 0.6670 -0.0420 5.0660 H 0 0 0 0 0 0 0 0 0 0 0 0 1 2 2 0 0 0 0 1 3 1 0 0 0 0 1 4 1 0 0 0 0 1 5 1 0 0 0 0 3 11 1 0 0 0 0 4 12 1 0 0 0 0 5 6 1 0 0 0 0 6 7 1 0 0 0 0 6 13 1 0 0 0 0 6 14 1 0 0 0 0 7 8 2 0 0 0 0 7 9 1 0 0 0 0 9 10 1 0 0 0 0 9 15 1 0 0 0 0 9 16 1 0 0 0 0 10 17 1 0 0 0 0 M END): 20 ms reading 17 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 17 atoms created ModelSet: not autobonding; use forceAutobond=true to force automatic bond creation Script completed Jmol script terminated
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| Dihydroxyacetone phosphate (DHAP, also glycerone phosphate in older texts) is the anion with the formula HOCH2C(O)CH2OPO32-. This anion is involved in many metabolic pathways, including the Calvin cycle in plants and glycolysis. It is the phosphate ester of dihydroxyacetone.
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Read full article at Wikipedia
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| InChI=1S/C3H7O6P/c4-1-3(5)2-9-10(6,7)8/h4H,1-2H2,(H2,6,7,8) |
| GNGACRATGGDKBX-UHFFFAOYSA-N |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
Saccharomyces cerevisiae metabolite
Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ).
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
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View more via ChEBI Ontology
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3-hydroxy-2-oxopropyl dihydrogen phosphate
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1,3-Dihydroxy-2-propanone monodihydrogen phosphate
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ChemIDplus
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1,3-Dihydroxy-2-propanone phosphate
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HMDB
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1,3-Dihydroxyacetone 1-phosphate
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HMDB
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1-hydroxy-3-(phosphonooxy)-2-Propanone
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HMDB
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1-hydroxy-3-(phosphonooxy)acetone
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ChemIDplus
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2-Propanone, 1-hydroxy-3-(phosphonooxy)-
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ChemIDplus
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3-hydroxy-2-oxopropyl phosphate
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IUBMB
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DHAP
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ChEBI
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dihydroxyacetone 3-phosphate
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ChemIDplus
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Dihydroxyacetone monophosphate
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HMDB
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Dihydroxyacetone phosphate
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KEGG COMPOUND
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glycerone monophosphate
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ChEBI
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Glycerone phosphate
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KEGG COMPOUND
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1708891
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Reaxys Registry Number
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Reaxys
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57-04-5
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CAS Registry Number
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KEGG COMPOUND
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57-04-5
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CAS Registry Number
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ChemIDplus
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Orozco JM, Krawczyk PA, Scaria SM, Cangelosi AL, Chan SH, Kunchok T, Lewis CA, Sabatini DM (2020)
Dihydroxyacetone phosphate signals glucose availability to mTORC1.
Nature metabolism 2, 893-901 [PubMed:32719541]
[show Abstract]
The mechanistic target of rapamycin complex 1 (mTORC1) kinase regulates cell growth by setting the balance between anabolic and catabolic processes. To be active, mTORC1 requires the environmental presence of amino acids and glucose. While a mechanistic understanding of amino acid sensing by mTORC1 is emerging, how glucose activates mTORC1 remains mysterious. Here, we used metabolically engineered human cells lacking the canonical energy sensor AMP-activated protein kinase to identify glucose-derived metabolites required to activate mTORC1 independent of energetic stress. We show that mTORC1 senses a metabolite downstream of the aldolase and upstream of the GAPDH-catalysed steps of glycolysis and pinpoint dihydroxyacetone phosphate (DHAP) as the key molecule. In cells expressing a triose kinase, the synthesis of DHAP from DHA is sufficient to activate mTORC1 even in the absence of glucose. DHAP is a precursor for lipid synthesis, a process under the control of mTORC1, which provides a potential rationale for the sensing of DHAP by mTORC1. | He Q, Toh JD, Ero R, Qiao Z, Kumar V, Serra A, Tan J, Sze SK, Gao YG (2020)
The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol.
The Plant journal : for cell and molecular biology 102, 153-164 [PubMed:31762135]
[show Abstract]
Dunaliella has been extensively studied due to its intriguing adaptation to high salinity. Its di-domain glycerol-3-phosphate dehydrogenase (GPDH) isoform is likely to underlie the rapid production of the osmoprotectant glycerol. Here, we report the structure of the chimeric Dunaliella salina GPDH (DsGPDH) protein featuring a phosphoserine phosphatase-like domain fused to the canonical glycerol-3-phosphate (G3P) dehydrogenase domain. Biochemical assays confirm that DsGPDH can convert dihydroxyacetone phosphate (DHAP) directly to glycerol, whereas a separate phosphatase protein is required for this conversion process in most organisms. The structure of DsGPDH in complex with its substrate DHAP and co-factor nicotinamide adenine dinucleotide (NAD) allows the identification of the residues that form the active sites. Furthermore, the structure reveals an intriguing homotetramer form that likely contributes to the rapid biosynthesis of glycerol. | Jacques B, Coinçon M, Sygusch J (2018)
Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
The Journal of biological chemistry 293, 7737-7753 [PubMed:29593097]
[show Abstract]
Crystal structures of two bacterial metal (Zn2+)-dependent d-fructose-1,6-bisphosphate (FBP) aldolases in complex with substrate, analogues, and triose-P reaction products were determined to 1.5-2.0 Å resolution. The ligand complexes cryotrapped in native or mutant Helicobacter pylori aldolase crystals enabled a novel mechanistic description of FBP C3-C4 bond cleavage. The reaction mechanism uses active site remodeling during the catalytic cycle, implicating relocation of the Zn2+ cofactor that is mediated by conformational changes of active site loops. Substrate binding initiates conformational changes triggered upon P1 phosphate binding, which liberates the Zn2+-chelating His-180, allowing it to act as a general base for the proton abstraction at the FBP C4 hydroxyl group. A second zinc-chelating His-83 hydrogen bonds the substrate C4 hydroxyl group and assists cleavage by stabilizing the developing negative charge during proton abstraction. Cleavage is concerted with relocation of the metal cofactor from an interior to a surface-exposed site, thereby stabilizing the nascent enediolate form. Conserved residue Glu-142 is essential for protonation of the enediolate form prior to product release. A d-tagatose 1,6-bisphosphate enzymatic complex reveals how His-180-mediated proton abstraction controls stereospecificity of the cleavage reaction. Recognition and discrimination of the reaction products, dihydroxyacetone-P and d-glyceraldehyde 3-P, occurs via charged hydrogen bonds between hydroxyl groups of the triose-Ps and conserved residues, Asp-82 and Asp-255, respectively, and are crucial aspects of the enzyme's role in gluconeogenesis. Conformational changes in mobile loops β5-α7 and β6-α8 (containing catalytic residues Glu-142 and His-180, respectively) drive active site remodeling, enabling the relocation of the metal cofactor. | Hartley CJ, French NG, Scoble JA, Williams CC, Churches QI, Frazer AR, Taylor MC, Coia G, Simpson G, Turner NJ, Scott C (2017)
Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis.
PloS one 12, e0184183 [PubMed:29112947]
[show Abstract]
Carbon-carbon bond formation is one of the most challenging reactions in synthetic organic chemistry, and aldol reactions catalysed by dihydroxyacetone phosphate-dependent aldolases provide a powerful biocatalytic tool for combining C-C bond formation with the generation of two new stereo-centres, with access to all four possible stereoisomers of a compound. Dihydroxyacetone phosphate (DHAP) is unstable so the provision of DHAP for DHAP-dependent aldolases in biocatalytic processes remains complicated. Our research has investigated the efficiency of several different enzymatic cascades for the conversion of glycerol to DHAP, including characterising new candidate enzymes for some of the reaction steps. The most efficient cascade for DHAP production, comprising a one-pot four-enzyme reaction with glycerol kinase, acetate kinase, glycerophosphate oxidase and catalase, was coupled with a DHAP-dependent fructose-1,6-biphosphate aldolase enzyme to demonstrate the production of several rare chiral sugars. The limitation of batch biocatalysis for these reactions and the potential for improvement using kinetic modelling and flow biocatalysis systems is discussed. | Deng S, Scott D, Myers D, Garg U (2016)
Quantification of Dihydroxyacetone Phosphate (DHAP) in Human Red Blood Cells by HPLC-TripleTOF 5600™ Mass Spectrometer.
Methods in molecular biology (Clifton, N.J.) 1378, 81-86 [PubMed:26602120]
[show Abstract]
Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). TPI deficiency results in accumulation of DHAP in human red blood cells and other tissues. The disease is characterized by congenital hemolytic anemia, and progressive neuromuscular dysfunction. The laboratory diagnosis is generally made by measurement of TPI activity in RBCs. Measurement of DHAP can be useful in further confirmation and follow-up of the disease. We developed HPLC/TOF-MS method for quantitation of DHAP in RBCs. The method involves simple protein precipitation, reverse phase C8 column chromatography, ion pairing with tributylamine, and long run time of 50 min to separate the two isomers (G3P and DHAP). | Tsuruoka M, Hara J, Hirayama A, Sugimoto M, Soga T, Shankle WR, Tomita M (2013)
Capillary electrophoresis-mass spectrometry-based metabolome analysis of serum and saliva from neurodegenerative dementia patients.
Electrophoresis 34, 2865-2872 [PubMed:23857558]
[show Abstract]
Despite increasing global prevalence, the precise pathogenesis and terms for objective diagnosis of neurodegenerative dementias remain controversial, and comprehensive understanding of the disease remains lacking. Here, we conducted metabolomic analysis of serum and saliva obtained from patients with neurodegenerative dementias (n = 10), including Alzheimer's disease, frontotemporal lobe dementia, and Lewy body disease, as well as from age-matched healthy controls (n = 9). Using CE-TOF-MS, six metabolites in serum (β-alanine, creatinine, hydroxyproline, glutamine, iso-citrate, and cytidine) and two in saliva (arginine and tyrosine) were significantly different between dementias and controls. Using multivariate analysis, serum was confirmed as a more efficient biological fluid for diagnosis compared to saliva; additionally, 45 metabolites in total were identified as candidate markers that could discriminate at least one pair of diagnostic groups from the healthy control group. These metabolites possibly provide an objective method for diagnosing dementia-type by multiphase screening. Moreover, diagnostic-type-dependent differences were observed in several tricarboxylic acid cycle compounds detected in serum, indicating that some pathways in glucose metabolism may be altered in dementia patients. This pilot study revealed novel alterations in metabolomic profiles between various neurodegenerative dementias, which would contribute to etiological investigations. | Slepokura K, Lis T (2010)
Dihydroxyacetone phosphate, DHAP, in the crystalline state: monomeric and dimeric forms.
Carbohydrate research 345, 512-529 [PubMed:20092811]
[show Abstract]
It was shown that dihydroxyacetone phosphate may exist in both monomeric DHAP (C(3)H(7)O(6)P) and dimeric DHAP-dimer (C(6)H(14)O(12)P(2)) form. Monomeric DHAP was obtained in the form of four crystalline salts: CaCl(DHAP) x 2.9H(2)O (7a), Ca(2)Cl(3)(DHAP) x 5H(2)O (7b), CaCl(DHAP) x 2H(2)O (7c), and CaBr(DHAP) x 5H(2)O (7d) by crystallization from aqueous solutions containing DHAP acid and CaCl(2) or CaBr(2), or by direct crystallization from a solution containing DHAP precursor and CaCl(2). At least one of the salts is stable and may be stored in the crystalline state at room temperature for several months. The dimeric form was obtained by slow saturation of free DHAP syrup with ammonia at -18 degrees C and isolated in the form of its hydrated diammonium salt (NH(4))(2)(DHAP-dimer) x 4H(2)O (8). The synthesis of the compounds, their crystallization, and crystal structures determined by X-ray crystallography are described. In all 7a-d monomeric DHAP exists in the monoanionic form in an extended (in-plane) cisoid conformation, with both hydroxyl and ester oxygen atoms being synperiplanar to the carbonyl O atom. The crucial structural feature is the coordination manner, in which the terminal phosphate oxygen atoms act as chelating as well as bridging atoms for the calcium cations. Additionally, the DHAP monoanions chelate another Ca(2+) by the alpha-hydroxycarbonyl moiety, in a manner observed previously in dihydroxyacetone (DHA) calcium chloride complexes. In dimeric 8 the anion is a trans isomer with the dioxane ring in a chair conformation with the hydroxyl groups in axial positions and the phosphomethyl group in an equatorial position. | Nakayama Y, Kinoshita A, Tomita M (2005)
Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition.
Theoretical biology & medical modelling 2, 18 [PubMed:15882454]
[show Abstract]
BackgroundCell simulation, which aims to predict the complex and dynamic behavior of living cells, is becoming a valuable tool. In silico models of human red blood cell (RBC) metabolism have been developed by several laboratories. An RBC model using the E-Cell simulation system has been developed. This prototype model consists of three major metabolic pathways, namely, the glycolytic pathway, the pentose phosphate pathway and the nucleotide metabolic pathway. Like the previous model by Joshi and Palsson, it also models physical effects such as osmotic balance. This model was used here to reconstruct the pathology arising from hereditary glucose-6-phosphate dehydrogenase (G6PD) deficiency, which is the most common deficiency in human RBC.ResultsSince the prototype model could not reproduce the state of G6PD deficiency, the model was modified to include a pathway for de novo glutathione synthesis and a glutathione disulfide (GSSG) export system. The de novo glutathione (GSH) synthesis pathway was found to compensate partially for the lowered GSH concentrations resulting from G6PD deficiency, with the result that GSSG could be maintained at a very low concentration due to the active export system.ConclusionThe results of the simulation were consistent with the estimated situation of real G6PD-deficient cells. These results suggest that the de novo glutathione synthesis pathway and the GSSG export system play an important role in alleviating the consequences of G6PD deficiency. | Schuster M (1999)
Homoisofagomines: chemical-enzymatic synthesis and evaluation as alpha- and beta-glucosidase inhibitors.
Bioorganic & medicinal chemistry letters 9, 615-618 [PubMed:10098675]
[show Abstract]
Methyl- and hydroxymethyl derivatives of the highly potent glycosidase inhibitor isofagomine are accessible via aldolase-catalyzed C-C bond formation and competitively inhibit beta-glucosidase at low micromolar concentrations. | Yamamoto T, Moriwaki Y, Takahashi S, Ohata H, Nakano T, Yamakita J, Higashino K (1996)
Effect of glucagon on the xylitol-induced increase in the plasma concentration and urinary excretion of purine bases.
Metabolism: clinical and experimental 45, 1354-1359 [PubMed:8931639]
[show Abstract]
To investigate whether glucagon affects the xylitol-induced increase in the production of purine bases (hypoxanthine, xanthine, and uric acid), the present study was performed with five healthy subjects. Intravenous administration of 300 mL 10% xylitol increased the plasma concentration and urinary excretion of purine bases, erythrocyte concentrations of adenosine monophosphate (AMP) and adenosine diphosphate (ADP), and blood concentrations of glyceraldehyde-3-phosphate (GA3P) + dihydroxyacetone phosphate (DHAP), fructose-1,6-bisphosphate (FBP), and lactic acid; it decreased the blood concentration of pyruvic acid and the plasma concentration and urinary excretion of inorganic phosphate. However, intravenous administration of 1 mg glucagon together with xylitol reduced the xylitol-induced changes in oxypurines, pyruvic acid, GABP + DHAP, and FBP, whereas it promoted the xylitol-induced increase in the urinary excretion of total purine bases and did not affect the xylitol-induced increase in the plasma concentration of total purine bases. In addition, in vitro study demonstrated that sodium pyruvate prevented the xylitol-induced degradation of adenine nucleotides in erythrocytes. These results suggested that gluconeogenesis due to glucagon increased the production of pyruvic acid, accelerated the conversion of NADH to NAD, and thereby prevented both the xylitol-induced degradation of adenine nucleotides in organs similar to erythrocytes and the inhibition of xanthine dehydrogenase in the liver and small intestine, resulting in decreases in the plasma concentration and urinary excretion of oxypurines. However, it was also suggested that in the liver storing glycogen, glucagon-induced glycogenolysis accumulated sugar phosphates, resulting in purine degradation, since the xylitol-induced increase in the NADH/NAD ratio partially blocked glycolysis at the level of GABP dehydrogenase. Therefore, administration of glucagon together with xylitol may synergistically increase purine degradation more than xylitol alone, despite decreases in the plasma concentration and urinary excretion of oxypurines. | Roberts NB, Dutton J, Helliwell T, Rothwell PJ, Kavanagh JP (1992)
Pyrophosphate in synovial fluid and urine and its relationship to urinary risk factors for stone disease.
Annals of clinical biochemistry 29 ( Pt 5), 529-534 [PubMed:1332571]
[show Abstract]
Inorganic pyrophosphate (PPi) measurement in urine and synovial fluid has been established using the PPi-dependent phosphorylation of fructose-6-phosphate and subsequent reduction of dihydroxyacetone phosphate by NADH. The assay is linear up to 200 mumol/L, easy to perform and gives results comparable to more complex methods. Daily urinary output of PPi was independently related to both age (P = 0.0014) and sex (P = 0.0002). Men had higher values than women and older individuals excreted greater amounts. Male stone formers, younger than 45 years, had lower values than age matched male controls (P = 0.012). Younger female stone formers also tended to have lower values. In stone formers' urine significant and independent correlations were found of PPi excretion with urine volume (P = 0.004) and with phosphate excretion (P = 0.008). Oxalate excretion and that of other urine constituents and the degree of supersaturation with common stone-forming salts were not correlated with PPi. PPi excretion was markedly elevated in the urine of two patients with hypophosphatasia. The PPi concentration in synovial fluid from painful, swollen knee joints was elevated, but unrelated to the presence or absence of PPi or urate crystals. | Schutgens RB, Wanders RJ, Heymans HS, Schram AW, Tager JM, Schrakamp G, van den Bosch H (1987)
Zellweger syndrome: biochemical procedures in diagnosis, prevention and treatment.
Journal of inherited metabolic disease 10 Suppl 1, 33-45 [PubMed:3119940]
[show Abstract]
In patients with cerebro-hepato-renal (Zellweger) syndrome, the absence of peroxisomes results in an impairment of metabolic processes in which peroxisomes are normally involved. These include the catabolism of very long chain (greater than C22) fatty acids, the biosynthesis of ether-phospholipids and of bile acids, the catabolism of phytanic acid and the catabolism of pipecolic acid. Many diagnostic tests for Zellweger syndrome have become available in recent years. In classic Zellweger syndrome abnormal C27-bile acids, very long chain fatty acids, dicarboxylic acids and pipecolic acid accumulate in the plasma of the patients. Moreover, depending upon the diet, plasma phytanic acid concentrations may be elevated. In platelets the activity of acyl-CoA: dihydroxyacetone phosphate acyltransferase is deficient; in erythrocytes from young (less than 4 months) patients the plasmalogen content of the phospholipids is decreased. In cultured fibroblasts from skin and from chorionic villus and cultured amniotic fluid cells from Zellweger patients the plasmalogen level is lowered; there is a decreased activity of acyl-CoA: dihydroxyacetone phosphate acyltransferase, alkyl dihydroxyacetonephosphate synthase and phytanic acid oxidase; the de novo biosynthesis of plasmalogens and the peroxisomal beta-oxidation of fatty acids are impaired and the intracellular localization of catalase is abnormal. Dietary treatment of patients with Zellweger syndrome has not so far resulted in an objective clinical improvement. As Zellweger syndrome is usually fatal in early life, prenatal diagnosis of the disease is important. |
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