2.0 2012-05-31 13:53:34 -0600 2015-09-13 12:56:11 -0600 ECMDB01494 M2MDB000402 Acetylphosphate Acetylphosphate is an intermediate in taurine and hypotaurine metabolism. It is generated from sulfoacetaldehyde, converted to acetyl-CoA and acetate via phosphate acetyltransferase (EC:2.3.1.8) and acetate kinase (EC:2.7.2.1) respectively. It is also intermediate in pyruvate metabolism. It is generated from pyruvate and the formation is catalyzed by pyruvate oxidase (EC:1.2.3.3). (KEGG) Acetyl phosphate Acetyl phosphoric acid Acetyl-P Acetylphosphate Acetylphosphoric acid C2H5O5P 140.0319 139.987459782 (acetyloxy)phosphonic acid acetylphosphate 590-54-5 CC(=O)OP(O)(O)=O InChI=1S/C2H5O5P/c1-2(3)7-8(4,5)6/h1H3,(H2,4,5,6) LIPOUNRJVLNBCD-UHFFFAOYSA-N Solid Cytosol logp -0.92 ALOGPS logs -0.90 ALOGPS solubility 1.78e+01 g/l ALOGPS logp -0.88 ChemAxon pka_strongest_acidic 1.24 ChemAxon pka_strongest_basic -7.4 ChemAxon iupac (acetyloxy)phosphonic acid ChemAxon average_mass 140.0319 ChemAxon mono_mass 139.987459782 ChemAxon smiles CC(=O)OP(O)(O)=O ChemAxon formula C2H5O5P ChemAxon inchi InChI=1S/C2H5O5P/c1-2(3)7-8(4,5)6/h1H3,(H2,4,5,6) ChemAxon inchikey LIPOUNRJVLNBCD-UHFFFAOYSA-N ChemAxon polar_surface_area 83.83 ChemAxon refractivity 23.8 ChemAxon polarizability 9.87 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge -2 ChemAxon formal_charge 0 ChemAxon Reductive carboxylate cycle (CO2 fixation) ec00720 Pyruvate metabolism ec00620 Methane metabolism ec00680 Propanoate metabolism Starting from L-threonine, this compound is deaminated through a threonine deaminase resulting in a hydrogen ion, a water molecule and a (2z)-2-aminobut-2-enoate. The latter compound then isomerizes to a 2-iminobutanoate, This compound then reacts spontaneously with hydrogen ion and a water molecule resulting in a ammonium and a 2-Ketobutyric acid. The latter compound interacts with CoA through a pyruvate formate-lyase / 2-ketobutyrate formate-lyase resulting in a formic acid and a propionyl-CoA. Propionyl-CoA can then be processed either into a 2-methylcitric acid or into a propanoyl phosphate. Propionyl-CoA interacts with oxalacetic acid and a water molecule through a 2-methylcitrate synthase resulting in a hydrogen ion, a CoA and a 2-Methylcitric acid.The latter compound is dehydrated through a 2-methylcitrate dehydratase resulting in a water molecule and cis-2-methylaconitate. The latter compound is then dehydrated by a bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase resulting in a water molecule and methylisocitric acid. The latter compound is then processed by 2-methylisocitrate lyase resulting in a release of succinic acid and pyruvic acid. Succinic acid can then interact with a propionyl-CoA through a propionyl-CoA:succinate CoA transferase resulting in a propionic acid and a succinyl CoA. Succinyl-CoA is then isomerized through a methylmalonyl-CoA mutase resulting in a methylmalonyl-CoA. This compound is then decarboxylated through a methylmalonyl-CoA decarboxylase resulting in a release of Carbon dioxide and Propionyl-CoA. ropionyl-CoA interacts with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. Propionyl-CoA can react with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. The latter compound is then dephosphorylated through a ADP driven acetate kinase/propionate kinase protein complex resulting in an ATP and Propionic acid. Propionic acid can be processed by a reaction with CoA through a ATP-driven propionyl-CoA synthetase resulting in a pyrophosphate, an AMP and a propionyl-CoA. PW000940 ec00640 Metabolic Taurine and hypotaurine metabolism ec00430 Microbial metabolism in diverse environments ec01120 Metabolic pathways eco01100 Acetate metabolism The acetate biosynthesis starts with acetyl-CoA reacting with phosphate through a phosphate acetyltransferase resulting in the release of a coenzyme A and an acetyl phosphate. The latter compound in turn reacts with ADP through an acetate kinase resulting in the release of an ATP and an acetate. The acetate reacts with ATP and coenzyme A through an acetyl-CoA synthase resulting in the release of a diphosphate, an AMP and an acetyl-CoA. Acetyl-CoA can be biosynthesized by acetoacetate reacting with an acetyl-CoA through an acetoacetyl-CoA transferase resulting in the release of an acetate and an acetoacetyl-CoA. The acetoacetyl-CoA reacts with an acetyl-CoA acetyltransferase resulting in the release of an coenzyme A and 2 acetyl-CoA PW002090 Metabolic acetate formation from acetyl-CoA I PWY0-1312 mixed acid fermentation FERMENTATION-PWY Specdb::CMs 8026 Specdb::CMs 174705 Specdb::NmrOneD 1719 Specdb::NmrOneD 147920 Specdb::NmrOneD 147921 Specdb::NmrOneD 147922 Specdb::NmrOneD 147923 Specdb::NmrOneD 147924 Specdb::NmrOneD 147925 Specdb::NmrOneD 147926 Specdb::NmrOneD 147927 Specdb::NmrOneD 147928 Specdb::NmrOneD 147929 Specdb::NmrOneD 147930 Specdb::NmrOneD 147931 Specdb::NmrOneD 147932 Specdb::NmrOneD 147933 Specdb::NmrOneD 147934 Specdb::NmrOneD 147935 Specdb::NmrOneD 147936 Specdb::NmrOneD 147937 Specdb::NmrOneD 147938 Specdb::NmrOneD 147939 Specdb::MsMs 1613 Specdb::MsMs 1614 Specdb::MsMs 1615 Specdb::MsMs 257304 Specdb::MsMs 257305 Specdb::MsMs 257306 Specdb::MsMs 277242 Specdb::MsMs 277243 Specdb::MsMs 277244 Specdb::MsMs 2364808 Specdb::MsMs 2364809 Specdb::MsMs 2364810 Specdb::MsMs 2597500 Specdb::MsMs 2597501 Specdb::MsMs 2597502 Specdb::NmrTwoD 1077 Specdb::NmrTwoD 1658 HMDB01494 186 181 C00227 15350 ACETYL-P UVW Keseler, 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. 21097882 Kanehisa, 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. 22080510 van 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. 17765195 Winder, 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. 18331064 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Libeer JC, Scharpe SL, Verkerk RM, Deprettere AJ, Schepens PJ: Simultaneous determination of p-aminobenzoic acid, acetyl-p-aminobenzoic acid and p-aminohippuric acid in serum and urine by capillary gas chromatography with use of a nitrogen-phosphorus detector. Clin Chim Acta. 1981 Sep 10;115(2):119-23. 6974621 Dowling TC, Frye RF, Zemaitis MA: Simultaneous determination of p-aminohippuric acid, acetyl-p-aminohippuric acid and iothalamate in human plasma and urine by high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl. 1998 Sep 25;716(1-2):305-13. 9824245 Costakel, O.; Kitzoulesco, I. The possibility of acetylphosphate synthesis in cancerous and noncancerous human serum at pH 4. Rev. sci. Med., Acad. rep. populaire Roumaine (1960), 5 7-10. http://hmdb.ca/system/metabolites/msds/000/001/356/original/HMDB01494.pdf?1358463422 Acetate kinase P0A6A3 ACKA_ECOLI ackA http://ecmdb.ca/proteins/P0A6A3.xml Phosphate acetyltransferase P0A9M8 PTA_ECOLI pta http://ecmdb.ca/proteins/P0A9M8.xml Acylphosphatase P0AB65 ACYP_ECOLI yccX http://ecmdb.ca/proteins/P0AB65.xml Propionate kinase P11868 TDCD_ECOLI tdcD http://ecmdb.ca/proteins/P11868.xml Phosphoribosylglycinamide formyltransferase 2 P33221 PURT_ECOLI purT http://ecmdb.ca/proteins/P33221.xml Ethanolamine utilization protein eutD P77218 EUTD_ECOLI eutD http://ecmdb.ca/proteins/P77218.xml Acetyl-CoA + Phosphate <> Acetylphosphate + Coenzyme A R00230 PHOSACETYLTRANS-RXN Acetic acid + Adenosine triphosphate <> Acetylphosphate + ADP R00315 ACETATEKIN-RXN Acetylphosphate + Water <> Acetic acid + Phosphate R00317 Adenosine triphosphate + Acetic acid > ADP + Acetylphosphate Acetyl-CoA + Inorganic phosphate > CoA + Acetylphosphate Acetyl-CoA + Phosphate > Coenzyme A + Acetylphosphate PW_R006095 Acetylphosphate + ADP > Adenosine triphosphate + Acetic acid PW_R006097 Acetyl-CoA + Phosphate <> Acetylphosphate + Coenzyme A Acetic acid + Adenosine triphosphate <> Acetylphosphate + ADP Acetic acid + Adenosine triphosphate <> Acetylphosphate + ADP Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucose Shake flask and filter culture 1070.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 4280000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerol Shake flask and filter culture 1050.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 4200000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetate Shake flask and filter culture 1560.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 6240000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621