2.02012-05-31 13:51:01 -06002015-09-13 12:56:11 -0600ECMDB01368M2MDB0003583-Mercaptopyruvic acid3-Mercaptopyruvic acid is an intermediate in the metabolism of Cysteine and the production of hydrogen sulfide. It is a substrate for3-mercaptopyruvate sulfurtransferase which catalyzes the following reaction: H+ + 3-Mercaptopyruvic acid <=> Pyruvic acid + Hydrogen sulfide.β-mercaptopyruvateβ-mercaptopyruvic acidβ-thiopyruvateβ-thiopyruvic acid3-Mercapto-pyruvate3-Mercapto-pyruvic acid3-Mercaptopyruvate3-Mercaptopyruvic acidb-3-mercapto-2-oxo-Propanoateb-3-mercapto-2-oxo-Propanoic acidb-Mercaptopyruvateb-Mercaptopyruvic acidb-Thiopyruvateb-Thiopyruvic acidBeta-3-Mercapto-2-oxo-propanoateBeta-3-Mercapto-2-oxo-propanoic acidBeta-MercaptopyruvateBeta-Mercaptopyruvic acidBeta-ThiopyruvateBeta-Thiopyruvic acidMercaptopyruvateMercaptopyruvic acidMercPyrThiopyruvateThiopyruvic acidβ-3-mercapto-2-oxo-Propanoateβ-3-mercapto-2-oxo-Propanoic acidβ-Mercaptopyruvateβ-Mercaptopyruvic acidβ-Thiopyruvateβ-Thiopyruvic acidC3H4O3S120.127119.9881146842-oxo-3-sulfanylpropanoic acidβ-mercaptopyruvic acid2464-23-5OC(=O)C(=O)CSInChI=1S/C3H4O3S/c4-2(1-7)3(5)6/h7H,1H2,(H,5,6)OJOLFAIGOXZBCI-UHFFFAOYSA-NSolidCytosollogp0.15logs-1.12solubility9.09e+00 g/llogp0.29pka_strongest_acidic2.91pka_strongest_basic-9.9iupac2-oxo-3-sulfanylpropanoic acidaverage_mass120.127mono_mass119.988114684smilesOC(=O)C(=O)CSformulaC3H4O3SinchiInChI=1S/C3H4O3S/c4-2(1-7)3(5)6/h7H,1H2,(H,5,6)inchikeyOJOLFAIGOXZBCI-UHFFFAOYSA-Npolar_surface_area54.37refractivity25.82polarizability10.15rotatable_bond_count2acceptor_count3donor_count2physiological_charge-1formal_charge0Cysteine and methionine metabolismec00270Metabolic pathwayseco01100Hydrogen Sulfide Biosynthesis IIt has long been known that many bacteria are able to produce hydrogen sulfide [Barrett87]. However, the physiological role of H2S in nonsulfur bacteria was unknown. A recent report has now shown that production of H2S serves to defend cells from antibiotics by mitigating oxidative stress.
This pathway is one of two pathways for hydrogen sulfide biosynthesis. Neither of the two activities have been shown biochemically for the E. coli enzymes. The function of AspC as a cysteine transaminase is hypothesized based on sequence similarity to mammalian enzymes. The function of SseA was determined based on the phenotype of an sseA null mutant, which does not produce hydrogen sulfide.PW002066Metabolichydrogen sulfide biosynthesisPWY0-1534Specdb::CMs12794Specdb::CMs38041Specdb::CMs134735Specdb::CMs142469Specdb::NmrOneD1689Specdb::MsMs1534Specdb::MsMs1535Specdb::MsMs1536Specdb::MsMs294094Specdb::MsMs294095Specdb::MsMs294096Specdb::MsMs334732Specdb::MsMs334733Specdb::MsMs334734Specdb::MsMs2256853Specdb::MsMs2258900Specdb::MsMs2259694Specdb::MsMs2677374Specdb::MsMs2677375Specdb::MsMs2677376Specdb::MsMs3028763Specdb::MsMs3028764Specdb::MsMs3028765Specdb::NmrTwoD1630HMDB013689896C00957162083-MERCAPTO-PYRUVATEKeseler, 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-D114.22080510Winder, 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 80:2939-2948.18331064http://hmdb.ca/system/metabolites/msds/000/001/230/original/HMDB01368.pdf?1358462125Aspartate aminotransferaseP00509AAT_ECOLIaspChttp://ecmdb.ca/proteins/P00509.xml3-mercaptopyruvate sulfurtransferaseP31142THTM_ECOLIsseAhttp://ecmdb.ca/proteins/P31142.xmlThiosulfate sulfurtransferase YnjEP78067YNJE_ECOLIynjEhttp://ecmdb.ca/proteins/P78067.xmlHydrogen cyanide + 3-Mercaptopyruvic acid + Cyanide <> Hydrogen ion + Pyruvic acid + ThiocyanateR03106MERCAPYSTRANS-RXNL-Cysteine + alpha-Ketoglutarate <> 3-Mercaptopyruvic acid + DL-Glutamic acidR008963-Mercaptopyruvic acid + Sulfite <> Thiosulfate + Pyruvic acidR03105Hydrogen cyanide + 3-Mercaptopyruvic acid <> Thiocyanate + Pyruvic acidR03106MERCAPYSTRANS-RXNHydrogen ion + 3-Mercaptopyruvic acid > Pyruvic acid + Hydrogen sulfideRXN0-6945Oxoglutaric acid + L-Cysteine > L-Glutamate + 3-Mercaptopyruvic acidCYSTEINE-AMINOTRANSFERASE-RXNHydrogen cyanide + 3-Mercaptopyruvic acid Hydrogen ion + Pyruvic acid + ThiocyanateMERCAPYSTRANS-RXN3-Mercaptopyruvic acid + Hydrogen cyanide > Pyruvic acid + Thiocyanate3-Mercaptopyruvic acid > Pyruvic acid + Hydrogen sulfidePW_R006040