2.02012-05-31 13:55:41 -06002015-06-03 15:54:14 -0600ECMDB02134M2MDB000441AminoacetoneThreonine dehydrogenase catalyzes the oxidation of threonine by NAD+ to glycine and acetyl-CoA (5), but when the ratio acetyl-CoA/CoA increases in nutritional deprivation (e.g., in diabetes) the enzyme produces AA. (Chem. Res. Toxicol., 14 (9), 1323 -1329, 2001); 1-Amino-(8CI,9CI)-2-propanone1-Amino-2-propanone1-Aminopropan-2-onea-AminoacetoneAlpha-AminoacetoneAmino-(6CI)-2-propanoneAmino-2-propanoneα-AminoacetoneC3H7NO73.093873.0527638511-aminopropan-2-oneα-aminoacetone298-08-8CC(=O)CNInChI=1S/C3H7NO/c1-3(5)2-4/h2,4H2,1H3BCDGQXUMWHRQCB-UHFFFAOYSA-NSolidCytosollogp-1.29logs0.86solubility5.28e+02 g/llogp-0.82pka_strongest_acidic17.3pka_strongest_basic7.84iupac1-aminopropan-2-oneaverage_mass73.0938mono_mass73.052763851smilesCC(=O)CNformulaC3H7NOinchiInChI=1S/C3H7NO/c1-3(5)2-4/h2,4H2,1H3inchikeyBCDGQXUMWHRQCB-UHFFFAOYSA-Npolar_surface_area43.09refractivity19.55polarizability7.71rotatable_bond_count1acceptor_count2donor_count1physiological_charge1formal_charge0Pyrimidine metabolismThe metabolism of pyrimidines begins with L-glutamine interacting with water molecule and a hydrogen carbonate through an ATP driven carbamoyl phosphate synthetase resulting in a hydrogen ion, an ADP, a phosphate, an L-glutamic acid and a carbamoyl phosphate. The latter compound interacts with an L-aspartic acid through a aspartate transcarbamylase resulting in a phosphate, a hydrogen ion and a N-carbamoyl-L-aspartate. The latter compound interacts with a hydrogen ion through a dihydroorotase resulting in the release of a water molecule and a 4,5-dihydroorotic acid. This compound interacts with an ubiquinone-1 through a dihydroorotate dehydrogenase, type 2 resulting in a release of an ubiquinol-1 and an orotic acid. The orotic acid then interacts with a phosphoribosyl pyrophosphate through a orotate phosphoribosyltransferase resulting in a pyrophosphate and an orotidylic acid. The latter compound then interacts with a hydrogen ion through an orotidine-5 '-phosphate decarboxylase, resulting in an release of carbon dioxide and an Uridine 5' monophosphate. The Uridine 5' monophosphate process to get phosphorylated by an ATP driven UMP kinase resulting in the release of an ADP and an Uridine 5--diphosphate.
Uridine 5-diphosphate can be metabolized in multiple ways in order to produce a Deoxyuridine triphosphate.
1.-Uridine 5-diphosphate interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in the release of a water molecule and an oxidized thioredoxin and an dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
2.-Uridine 5-diphosphate interacts with a reduced NrdH glutaredoxin-like protein through a Ribonucleoside-diphosphate reductase 1 resulting in a release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
3.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate. The latter compound interacts with a reduced flavodoxin through ribonucleoside-triphosphate reductase resulting in the release of an oxidized flavodoxin, a water molecule and a Deoxyuridine triphosphate
4.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in the release of a water molecule, an oxidized flavodoxin and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
5.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP then interacts with a reduced NrdH glutaredoxin-like protein through a ribonucleoside-diphosphate reductase 2 resulting in the release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
6.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
The deoxyuridine triphosphate then interacts with a water molecule through a nucleoside triphosphate pyrophosphohydrolase resulting in a release of a hydrogen ion, a phosphate and a dUMP. The dUMP then interacts with a methenyltetrahydrofolate through a thymidylate synthase resulting in a dihydrofolic acid and a 5-thymidylic acid. Then 5-thymidylic acid is then phosphorylated through a nucleoside diphosphate kinase resulting in the release of an ADP and thymidine 5'-triphosphate.PW000942ec00240MetabolicGlycine, serine and threonine metabolismec00260Collection of Reactions without pathwaysPW001891MetabolicL-threonine degradation to methylglyoxalL-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways.PW002106Metabolicthreonine degradation III (to methylglyoxal)THRDLCTCAT-PWYSpecdb::CMs3013Specdb::CMs170225Specdb::NmrOneD109498Specdb::NmrOneD109499Specdb::NmrOneD109500Specdb::NmrOneD109501Specdb::NmrOneD109502Specdb::NmrOneD109503Specdb::NmrOneD109504Specdb::NmrOneD109505Specdb::NmrOneD109506Specdb::NmrOneD109507Specdb::NmrOneD109508Specdb::NmrOneD109509Specdb::NmrOneD109510Specdb::NmrOneD109511Specdb::NmrOneD109512Specdb::NmrOneD109513Specdb::NmrOneD109514Specdb::NmrOneD109515Specdb::NmrOneD109516Specdb::NmrOneD109517Specdb::MsMs19982Specdb::MsMs19983Specdb::MsMs19984Specdb::MsMs21533Specdb::MsMs21534Specdb::MsMs21535Specdb::MsMs2766047Specdb::MsMs2766048Specdb::MsMs2766049Specdb::MsMs2943166Specdb::MsMs2943167Specdb::MsMs2943168HMDB02134215210C0188817906AMINO-ACETONEGLM1-Amino-2-propanoneKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Thiele I, Swainston N, Fleming RM, Hoppe A, Sahoo S, Aurich MK, Haraldsdottir H, Mo ML, Rolfsson O, Stobbe MD, Thorleifsson SG, Agren R, Bolling C, Bordel S, Chavali AK, Dobson P, Dunn WB, Endler L, Hala D, Hucka M, Hull D, Jameson D, Jamshidi N, Jonsson JJ, Juty N, Keating S, Nookaew I, Le Novere N, Malys N, Mazein A, Papin JA, Price ND, Selkov E Sr, Sigurdsson MI, Simeonidis E, Sonnenschein N, Smallbone K, Sorokin A, van Beek JH, Weichart D, Goryanin I, Nielsen J, Westerhoff HV, Kell DB, Mendes P, Palsson BO: A community-driven global reconstruction of human metabolism. Nat Biotechnol. 2013 Mar 3. doi: 10.1038/nbt.2488.23455439Dutra F, Knudsen FS, Curi D, Bechara EJ: Aerobic oxidation of aminoacetone, a threonine catabolite: iron catalysis and coupled iron release from ferritin. Chem Res Toxicol. 2001 Sep;14(9):1323-9.11559049Karge E, Klinger W: [Effect of the pH value on the dissociation of the aminoketones delta-aminolevulinic acid and aminoacetone by extraction with ether and dichlormethane] Z Med Lab Diagn. 1981;22(6):358-9.7342529Kazachkov M, Yu PH: A novel HPLC procedure for detection and quantification of aminoacetone, a precursor of methylglyoxal, in biological samples. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Sep 25;824(1-2):116-22.16046286Turner, J. M. Aminoacetone production by microorganisms. Biochemical Journal (1966), 98(1), 7P.Glycerol dehydrogenaseP0A9S5GLDA_ECOLIgldAhttp://ecmdb.ca/proteins/P0A9S5.xmlPrimary amine oxidaseP46883AMO_ECOLItynAhttp://ecmdb.ca/proteins/P46883.xmlNADP-dependent L-serine/L-allo-threonine dehydrogenase ydfGP39831YDFG_ECOLIydfGhttp://ecmdb.ca/proteins/P39831.xmlAminoacetone + Hydrogen ion + NADH <> 1-Amino-2-propanol + NADAMINOPROPDEHYDROG-RXNL-2-Amino-3-oxobutanoic acid + Hydrogen ion > Aminoacetone + Carbon dioxideTHREOSPON-RXNAminoacetone + Water + Oxygen <> Pyruvaldehyde + Ammonia + Hydrogen peroxideR02529Aminoacetone + Water + Oxygen > Hydrogen ion + Pyruvaldehyde + Ammonia + Hydrogen peroxideR02529AMACETOXID-RXN1-Amino-2-propanol + NAD < Hydrogen ion + Aminoacetone + NADHAMINOPROPDEHYDROG-RXNL-Allothreonine + NADP + L-2-Amino-3-oxobutanoic acid <> Aminoacetone + Carbon dioxide + NADPH + Hydrogen ionR10852 1-Amino-2-propanol + NAD + 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene < NADH + Hydrogen ion + AminoacetonePW_R005365Aminoacetone + Oxygen + Water > Hydrogen peroxide + Ammonium + PyruvaldehydePW_R006139