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| 6-hydroxynicotinic acid |
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| CHEBI:16168 |
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| A monohydroxypyridine that is the 6-hydroxy derivative of nicotinic acid. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:2200, CHEBI:12219, CHEBI:20731
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| ZINC000000895988 |
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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__896209750245636__ initializing getValue debug = null getValue logLevel = null getValue allowjavascript = null AppletRegistry.checkIn(jmolApplet0_object__896209750245636__) 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:12219","platform":"J.awtjs2d.Platform","fullName":"jmolApplet0_object__896209750245636__","display":"jmolApplet0_canvas2d","signedApplet":"true","appletReadyCallback":"Jmol._readyCallback","statusListener":"[J.appletjs.Jmol.MyStatusListener object]","codeBase":"https://www.ebi.ac.uk/chebi/javascripts/jsmol/","syncId":"896209750245636","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__896209750245636__ 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 OA7 - Ideal conformer Mrv1927 06162116233D starting HoverWatcher_5 Time for openFile(OA7 - Ideal conformer Mrv1927 06162116233D 15 15 0 0 0 0 999 V2000 -0.0900 1.2570 0.0080 C 0 0 0 0 0 0 0 0 0 0 0 0 -1.4580 1.2030 0.0100 C 0 0 0 0 0 0 0 0 0 0 0 0 -2.0930 -0.0350 0.0180 C 0 0 0 0 0 0 0 0 0 0 0 0 -0.0760 -1.1550 0.0110 C 0 0 0 0 0 0 0 0 0 0 0 0 0.6270 0.0510 0.0090 C 0 0 0 0 0 0 0 0 0 0 0 0 2.1020 0.0570 -0.0050 C 0 0 0 0 0 0 0 0 0 0 0 0 -1.3930 -1.1600 0.0230 N 0 0 0 0 0 0 0 0 0 0 0 0 -3.4470 -0.0910 0.0200 O 0 0 0 0 0 0 0 0 0 0 0 0 2.7800 -1.1070 -0.0160 O 0 0 0 0 0 0 0 0 0 0 0 0 2.7050 1.1120 -0.0070 O 0 0 0 0 0 0 0 0 0 0 0 0 0.4260 2.2060 0.0020 H 0 0 0 0 0 0 0 0 0 0 0 0 -2.0390 2.1130 0.0060 H 0 0 0 0 0 0 0 0 0 0 0 0 0.4630 -2.0900 0.0100 H 0 0 0 0 0 0 0 0 0 0 0 0 3.7460 -1.0520 -0.0240 H 0 0 0 0 0 0 0 0 0 0 0 0 -3.8410 -0.1120 -0.8630 H 0 0 0 0 0 0 0 0 0 0 0 0 10 6 2 0 0 0 0 9 6 1 0 0 0 0 6 5 1 0 0 0 0 4 5 1 0 0 0 0 4 7 2 0 0 0 0 5 1 2 0 0 0 0 7 3 1 0 0 0 0 1 2 1 0 0 0 0 3 2 2 0 0 0 0 3 8 1 0 0 0 0 1 11 1 0 0 0 0 2 12 1 0 0 0 0 4 13 1 0 0 0 0 9 14 1 0 0 0 0 8 15 1 0 0 0 0 M END): 17 ms reading 15 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 15 atoms created ModelSet: not autobonding; use forceAutobond=true to force automatic bond creation Script completed Jmol script terminated
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| InChI=1S/C6H5NO3/c8-5-2-1-4(3-7-5)6(9)10/h1-3H,(H,7,8)(H,9,10) |
| BLHCMGRVFXRYRN-UHFFFAOYSA-N |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Arabidopsis thaliana
(NCBI:txid3702)
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Found in
leaf
(BTO:0000713).
See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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Found in
urine
(BTO:0001419).
See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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From MetaboLights
See:
MetaboLights Study
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human urinary metabolite
Any metabolite (endogenous or exogenous) found in human urine samples.
Arabidopsis thaliana metabolite
Any plant metabolite that is produced by Arabidopsis thaliana.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
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View more via ChEBI Ontology
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6-hydroxypyridine-3-carboxylic acid
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6-Hydroxynicotinate
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KEGG COMPOUND
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6-Hydroxynicotinic acid
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KEGG COMPOUND
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115991
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Reaxys Registry Number
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Reaxys
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5006-66-6
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CAS Registry Number
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NIST Chemistry WebBook
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5006-66-6
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CAS Registry Number
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ChemIDplus
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Nakamoto KD, Perkins SW, Campbell RG, Bauerle MR, Gerwig TJ, Gerislioglu S, Wesdemiotis C, Anderson MA, Hicks KA, Snider MJ (2019)
Mechanism of 6-Hydroxynicotinate 3-Monooxygenase, a Flavin-Dependent Decarboxylative Hydroxylase Involved in Bacterial Nicotinic Acid Degradation.
Biochemistry 58, 1751-1763 [PubMed:30810301]
[show Abstract]
6-Hydroxynicotinate 3-monooxygenase (NicC) is a Group A FAD-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH in nicotinic acid degradation by aerobic bacteria. Two mechanisms for the decarboxylative hydroxylation half-reaction have been proposed [Hicks, K., et al. (2016) Biochemistry 55, 3432-3446]. Results with Bordetella bronchiseptica RB50 NicC here show that a homocyclic analogue of 6-HNA, 4-hydroxybenzoic acid (4-HBA), is decarboxylated and hydroxylated by NicC with a 420-fold lower catalytic efficiency than is 6-HNA. The 13( V/ K), measured with wild-type NicC by isotope ratio mass spectrometry following the natural abundance of 13C in the CO2 product, is inverse for both 6-HNA (0.9989 ± 0.0002) and 4-HBA (0.9942 ± 0.0004) and becomes negligible (0.9999 ± 0.0004) for 5-chloro-6-HNA, an analogue that is 10-fold more catalytically efficient than 6-HNA. Covalently bound 6-HNA complexes of NicC are not observed by mass spectrometry. Comparative steady-state kinetic and Kd6HNA analyses of active site NicC variants (C202A, H211A, H302A, H47E, Y215F, and Y225F) identify Tyr215 and His47 as critical determinants both of 6-HNA binding ( KdY215F/ KdWT > 240; KdH47E/ KdWT > 350) and in coupling rates of 2,5-DHP and NAD+ product formation ([2,5-DHP]/[NAD+] = 1.00 (WT), 0.005 (Y215F), and 0.07 (H47E)]. Results of these functional analyses are in accord with an electrophilic aromatic substitution reaction mechanism in which His47-Tyr215 may serve as the general base to catalyze substrate hydroxylation and refine the structural model for substrate binding by NicC. | Booth WT, Davis RR, Deora R, Hollis T (2019)
Structural mechanism for regulation of DNA binding of BpsR, a Bordetella regulator of biofilm formation, by 6-hydroxynicotinic acid.
PloS one 14, e0223387 [PubMed:31697703]
[show Abstract]
Bordetella bacteria are respiratory pathogens of humans, birds, and livestock. Bordetella pertussis the causative agent of whopping cough remains a significant health issue. The transcriptional regulator, BpsR, represses a number of Bordetella genes relating to virulence, cell adhesion, cell motility, and nicotinic acid metabolism. DNA binding of BpsR is allosterically regulated by interaction with 6-hydroxynicotinic acid (6HNA), the first product in the nicotinic acid degradation pathway. To understand the mechanism of this regulation, we have determined the crystal structures of BpsR and BpsR in complex with 6HNA. The structures reveal that BpsR binding of 6HNA induces a conformational change in the protein to prevent DNA binding. We have also identified homologs of BpsR in other Gram negative bacteria in which the amino acids involved in recognition of 6HNA are conserved, suggesting a similar mechanism for regulating nicotinic acid degradation. | Roux A, Xu Y, Heilier JF, Olivier MF, Ezan E, Tabet JC, Junot C (2012)
Annotation of the human adult urinary metabolome and metabolite identification using ultra high performance liquid chromatography coupled to a linear quadrupole ion trap-Orbitrap mass spectrometer.
Analytical chemistry 84, 6429-6437 [PubMed:22770225]
[show Abstract]
Metabolic profiles of biofluids obtained by atmospheric pressure ionization mass spectrometry-based technologies contain hundreds to thousands of features, most of them remaining unknown or at least not characterized in analytical systems. We report here on the annotation of the human adult urinary metabolome and metabolite identification from electrospray ionization mass spectrometry (ESI-MS)-based metabolomics data sets. Features of biological interest were first of all annotated using the ESI-MS database of the laboratory. They were also grouped, thanks to software tools, and annotated using public databases. Metabolite identification was achieved using two complementary approaches: (i) formal identification by matching chromatographic retention times, mass spectra, and also product ion spectra (if required) of metabolites to be characterized in biological data sets to those of reference compounds and (ii) putative identification from biological data thanks to MS/MS experiments for metabolites not available in our chemical library. By these means, 384 metabolites corresponding to 1484 annotated features (659 in negative ion mode and 825 in positive ion mode) were characterized in human urine samples. Of these metabolites, 192 and 66 were formally and putatively identified, respectively, and 54 are reported in human urine for the first time. These lists of features could be used by other laboratories to annotate their ESI-MS metabolomics data sets. | Gronwald W, Klein MS, Zeltner R, Schulze BD, Reinhold SW, Deutschmann M, Immervoll AK, Böger CA, Banas B, Eckardt KU, Oefner PJ (2011)
Detection of autosomal dominant polycystic kidney disease by NMR spectroscopic fingerprinting of urine.
Kidney international 79, 1244-1253 [PubMed:21389975]
[show Abstract]
Autosomal dominant polycystic kidney disease (ADPKD) is a frequent cause of kidney failure; however, urinary biomarkers for the disease are lacking. In a step towards identifying such markers, we used multidimensional-multinuclear nuclear magnetic resonance (NMR) spectroscopy with support vector machine-based classification and analyzed urine specimens of 54 patients with ADPKD and slightly reduced estimated glomerular filtration rates. Within this cohort, 35 received medication for arterial hypertension and 19 did not. The results were compared with NMR profiles of 46 healthy volunteers, 10 ADPKD patients on hemodialysis with residual renal function, 16 kidney transplant patients, and 52 type 2 diabetic patients with chronic kidney disease. Based on the average of 51 out of 701 NMR features, we could reliably discriminate ADPKD patients with moderately advanced disease from ADPKD patients with end-stage renal disease, patients with chronic kidney disease of other etiologies, and healthy probands with an accuracy of >80%. Of the 35 patients with ADPKD receiving medication for hypertension, most showed increased excretion of proteins and also methanol. In contrast, elevated urinary methanol was not found in any of the control and other patient groups. Thus, we found that NMR fingerprinting of urine differentiates ADPKD from several other kidney diseases and individuals with normal kidney function. The diagnostic and prognostic potential of these profiles requires further evaluation. | Yang Y, Yuan S, Dai Y, Shang G (2008)
[Microplate for high throughput screening of 6-hydroxynicotinic acid transforming strains].
Wei sheng wu xue bao = Acta microbiologica Sinica 48, 112-115 [PubMed:18338586]
[show Abstract]
Recently, new insecticides containing 3-chloropyridylmethyl group as a versatile building block have been developed, among which imidachloprid is a promising one. The synthesis of imidachloprid can use 6-Hydroxynicotinic acid, the first intermediate of the bacterial degradation of nicotinic acid, as a starting material. It is difficult to hydroxylate nicotinic acid at C6 position in a chemical synthesis. However, biotransformation can produce 6-hydroxynicotinic acid with industrial application possibility. Therefore, methods for large scale screening of 6-hydroxynicotinic acid-producing microorganisms are urgent. A high through-put screening method for 6-hydroxynicotinic acid transforming strains was established by determining 6-hydroxynicotinic acid based on 96-well Microplate-Multiskan Spectrum. The determination wavelength and the reference wavelength of 6-hydroxynicotinic acid were 251nm and 231nm respectively. Beer's law is obeyed in the range of 0.5-11 microg/mL (R2 = 0.9999) for measuring 6-hydroxynicotinic acid. The average recovery rate was 99.11%-100.81%. The results showed that there was no apparent difference between our microplate method and previous HPLC method in the detecting 6-hydroxynicotinic acid formation. The microplate method is simple, convenient and accurate. It has the potential for large scale (about 2000 - 5000 reactions/d) screening of 6-hydroxynicotinic acid-producing microorganisms. | Gupta A, Dwivedi M, Nagana Gowda GA, Ayyagari A, Mahdi AA, Bhandari M, Khetrapal CL (2005)
(1)H NMR spectroscopy in the diagnosis of Pseudomonas aeruginosa-induced urinary tract infection.
NMR in biomedicine 18, 293-299 [PubMed:15759292]
[show Abstract]
The utility of (1)H NMR spectroscopy is suggested and demonstrated for the diagnosis of Pseudomonas aeruginosa in urinary tract infection (UTI). The specific property of P. aeruginosa of metabolizing nicotinic acid to 6-hydroxynicotinic acid (6-OHNA) is exploited. The quantity of 6-OHNA produced correlates well with the viable bacterial count. Other common bacteria causing UTI such as Escherichia coli, Klebsiella pneumonia, Enterobacter aerogenes, Acinetobacter baumanii, Proteus mirabilis, Citrobacter frundii, Enterococcus faecalis, Streptococcus gp B and Staphylococcus aureus do not metabolize nicotinic acid under similar conditions. The method provides a single-step documentation of P. aeruginosa qualitatively as well as quantitatively. The NMR method is demonstrated on urine samples from 30 patients with UTI caused by P. aeruginosa. | Shiraishi S, Sakamoto N, Maeda K, Ohki T, Hosoi M, Ohta K, Yamanaka N (1985)
Availability of 6-hydroxynicotinic acid for rapid identification of Pseudomonas aeruginosa and Serratia marcescens.
Journal of chromatography 338, 51-59 [PubMed:3926801]
[show Abstract]
Gas chromatography--mass spectrometry has been used to identify specific metabolites produced by Gram-negative bacteria such as Pseudomonas aeruginosa, Serratia marcescens, Klebsiella pneumoniae and Escherichia coli in a defined medium. 6-Hydroxynicotinic acid was detected in spent culture media of Pseudomonas aeruginosa and Serratia marcescens, but could not be detected in those of Klebsiella pneumoniae and Escherichia coli. The production of 6-hydroxynicotinic acid was recognized by the addition of nicotinic acid in urine with Pseudomonas aeruginosa or Serratia marcescens, but not without the addition of nicotinic acid. Among 10(5) Pseudomonas aeruginosa per 1 ml of urine (criteria for the diagnosis of urinary tract infection), 0.15 microgram of 6-hydroxynicotinic acid was detected in urine at 4 h incubation with nicotinic acid at the optimum pH of 6.9, 38 degrees C. The production of 6-hydroxynicotinic acid was proportional to the number of the bacteria and displayed a time dependency. These results suggest that the availability of 6-hydroxynicotinic acid might make for more rapid identification of bacteria than current methods. | Hirschberg R, Ensign JC (1972)
Oxidation of nicotinic acid by a Bacillus species: regulation of nicotinic acid and 6-hydroxynicotinic acid hydroxylases.
Journal of bacteriology 112, 392-397 [PubMed:5079068]
[show Abstract]
The first two enzymes employed by a Bacillus species for the dissimilation of nicotinic acid are coordinately induced. The inducer of the enzymes appears to be 6-hydroxynicotinic acid, the product of the first enzyme in the pathways. Synthesis of the enzymes is repressed by glucose when ammonium is present in the medium, but not when nicotinic acid is the sole nitrogen source. The possible significance of the coordinate induction and unusual repression is discussed. | Hirschberg R, Ensign JC (1971)
Oxidation of nicotinic acid by a Bacillus species: purification and properties of nicotinic acid and 6-hydroxynicotinic acid hydroxylases.
Journal of bacteriology 108, 751-756 [PubMed:5128334]
[show Abstract]
The enzymes of a Bacillus species that hydroxylate nicotinic acid to 6-hydroxynicotinic acid and 6-hydroxynicotinic acid to 2,6-dihydroxynicotinic acid were purified and characterized. The purified enzymes contained approximately two molecules of flavine and eight molecules of iron per molecule of enzyme. The enzymes were large (molecular weight, 400,000 to 450,000) and appeared to consist of subunits. | Hirschberg R, Ensign JC (1971)
Oxidation of nicotinic acid by a Bacillus species: source of oxygen atoms for the hydroxylation of nicotinic acid and 6-hydroxynicotinic acid.
Journal of bacteriology 108, 757-759 [PubMed:5128335]
[show Abstract]
Three types of evidence are presented to show that the enzymes that hydroxylate nicotinic acid to 2,6-dihydroxynicotinic acid use water as a source of oxygen atoms. (18)O is incorporated into the products from H(2) (18)O. Molecular oxygen acts as a terminal electron acceptor, one-half molecule being consumed per molecule of hydroxyl groups incorporated. An external electron acceptor is required for activity in purified preparations. | Chen TM (1970)
Electron spin resonance studies of the excited triplet states of DL-5-hydroxytryptophan, 5-hydroxyindole, 6-hydroxynicotinic acid, indole and hippuric acid.
Photochemistry and photobiology 12, 81-90 [PubMed:5498533] | Holcenberg JS, Tsai L (1969)
Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of 6-hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid.
The Journal of biological chemistry 244, 1204-1211 [PubMed:5767303] | HARARY I (1957)
Bacterial fermantation of nicotinic acid. II. Anaerobic reversible hydroxylation of nicotinic acid to 6-hydroxynicotinic acid.
The Journal of biological chemistry 227, 823-831 [PubMed:13463004] | HUGHES DE (1955)
6-Hydroxynicotinic acid as an intermediate in the oxidation of nicotinic acid by Pseudomonas fluorescens.
The Biochemical journal 60, 303-310 [PubMed:14389240] |
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