2.02012-05-31 10:24:56 -06002015-09-13 12:56:07 -0600ECMDB00251M2MDB000106TaurineTaurine is a sulfur amino acid like methionine, cystine, cysteine and homocysteine. It is a lesser-known amino acid because it is not incorporated into the structural building blocks of protein. Taurine has many diverse biological functions serving as a stabilizer of cell membranes and a facilitator in the transport of ions such as sodium, potassium, calcium and magnesium.1-Aminoethane-2-sulfonate1-Aminoethane-2-sulfonic acid1-Aminoethane-2-sulphonate1-Aminoethane-2-sulphonic acid2-Aminoethanesulfonate2-Aminoethanesulfonic acid2-Aminoethanesulphonate2-Aminoethanesulphonic acid2-Aminoethylsulfonate2-Aminoethylsulfonic acid2-Aminoethylsulphonate2-Aminoethylsulphonic acid2-Sulfoethylamine2-SulphoethylamineAminoethylsulfonateAminoethylsulfonic acidAminoethylsulphonateAminoethylsulphonic acidAminoetylsulfonateAminoetylsulfonic acidAminoetylsulphonateAminoetylsulphonic acidB-AminoethylsulfonateB-Aminoethylsulfonic acidB-AminoethylsulphonateB-Aminoethylsulphonic acidBeta-AminoethylsulfonateBeta-Aminoethylsulfonic acidBeta-AminoethylsulphonateBeta-Aminoethylsulphonic acidEthylaminesulfonateEthylaminesulfonic acidEthylaminesulphonateEthylaminesulphonic acidTaufonTauphonTaurineβ-Aminoethylsulfonateβ-Aminoethylsulfonic acidβ-Aminoethylsulphonateβ-Aminoethylsulphonic acidC2H7NO3S125.147125.0146637852-aminoethane-1-sulfonic acidtaurine107-35-7NCCS(O)(=O)=OInChI=1S/C2H7NO3S/c3-1-2-7(4,5)6/h1-3H2,(H,4,5,6)XOAAWQZATWQOTB-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmlogp-2.19logs-0.08solubility1.05e+02 g/lmelting_point300 oClogp-2.6pka_strongest_acidic-1.5pka_strongest_basic9.34iupac2-aminoethane-1-sulfonic acidaverage_mass125.147mono_mass125.014663785smilesNCCS(O)(=O)=OformulaC2H7NO3SinchiInChI=1S/C2H7NO3S/c3-1-2-7(4,5)6/h1-3H2,(H,4,5,6)inchikeyXOAAWQZATWQOTB-UHFFFAOYSA-Npolar_surface_area80.39refractivity24.61polarizability10.82rotatable_bond_count2acceptor_count4donor_count2physiological_charge0formal_charge0Sulfur metabolismThe sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion.
The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described.
The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000922ec00920MetabolicTaurine and hypotaurine metabolismec00430ABC transportersec02010Taurine Metabolism
Taurine is incorporated into the cytoplasm through a taurine ABC transporter. Once inside the cytoplasm, taurine interacts with an oxoglutaric acid and an oxygen through a taurine dioxygenase resulting in the release of succinic acid, sulfite , aminoacetaldehyde and carbon dioxidePW000774MetabolicTaurine Metabolism I Taurine is incorporated into the cytoplasm through a taurine ABC transporter. Once inside the cytoplasm, taurine interacts with an oxoglutaric acid and an oxygen through a taurine dioxygenase resulting in the release of succinic acid, sulfite , aminoacetaldehyde and carbon dioxidePW001028Metabolicinner membrane transportlist of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports addedPW000786Metabolicsulfur metabolism (butanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000923Metabolicsulfur metabolism (ethanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case ethanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Ethanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000925Metabolicsulfur metabolism (isethionate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case isethionate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Isethionate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000926Metabolicsulfur metabolism (methanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case methanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Methanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000927Metabolicsulfur metabolism (propanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 3-(N-morpholino)propanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 3-(N-morpholino)propanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000924Metabolictaurine degradation IVPWY0-981Specdb::CMs487Specdb::CMs488Specdb::CMs489Specdb::CMs2519Specdb::CMs30234Specdb::CMs30698Specdb::CMs30763Specdb::CMs32381Specdb::CMs32383Specdb::CMs166328Specdb::EiMs1313Specdb::NmrOneD1218Specdb::NmrOneD1277Specdb::NmrOneD2107Specdb::NmrOneD4964Specdb::NmrOneD6272Specdb::NmrOneD6273Specdb::NmrOneD6274Specdb::NmrOneD6275Specdb::NmrOneD6276Specdb::NmrOneD6277Specdb::NmrOneD6278Specdb::NmrOneD6279Specdb::NmrOneD6280Specdb::NmrOneD6281Specdb::NmrOneD6282Specdb::NmrOneD6283Specdb::NmrOneD6284Specdb::NmrOneD6285Specdb::NmrOneD6286Specdb::NmrOneD6287Specdb::NmrOneD6288Specdb::NmrOneD6289Specdb::NmrOneD6290Specdb::NmrOneD6291Specdb::NmrOneD166456Specdb::MsMs3750Specdb::MsMs3751Specdb::MsMs3752Specdb::MsMs3753Specdb::MsMs3754Specdb::MsMs3755Specdb::MsMs3756Specdb::MsMs3757Specdb::MsMs3758Specdb::MsMs3759Specdb::MsMs3760Specdb::MsMs3761Specdb::MsMs3762Specdb::MsMs438486Specdb::MsMs438487Specdb::MsMs438488Specdb::MsMs438489Specdb::MsMs438490Specdb::MsMs438753Specdb::MsMs438754Specdb::MsMs438755Specdb::MsMs438838Specdb::MsMs438839Specdb::MsMs438840Specdb::MsMs440022Specdb::NmrTwoD1007Specdb::NmrTwoD1238HMDB0025111231091C0024515891TAURINETAUTaurineKeseler, 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 80:2939-2948.18331064Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.19212411Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50.12834252Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7.6198473Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14.15911239Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6.12297216Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24.14992292Khan SA, Cox IJ, Hamilton G, Thomas HC, Taylor-Robinson SD: In vivo and in vitro nuclear magnetic resonance spectroscopy as a tool for investigating hepatobiliary disease: a review of H and P MRS applications. Liver Int. 2005 Apr;25(2):273-81.15780050Vinton NE, Laidlaw SA, Ament ME, Kopple JD: Taurine concentrations in plasma, blood cells, and urine of children undergoing long-term total parenteral nutrition. Pediatr Res. 1987 Apr;21(4):399-403.3106924Gonzalez-Quevedo A, Obregon F, Fernandez R, Santiesteban R, Serrano C, Lima L: Amino acid levels and ratios in serum and cerebrospinal fluid of patients with optic neuropathy in Cuba. Nutr Neurosci. 2001;4(1):51-62.11842876Schneider SM, Joly F, Gehrardt MF, Badran AM, Myara A, Thuillier F, Coudray-Lucas C, Cynober L, Trivin F, Messing B: Taurine status and response to intravenous taurine supplementation in adults with short-bowel syndrome undergoing long-term parenteral nutrition: a pilot study. Br J Nutr. 2006 Aug;96(2):365-70.16923232McCarty MF: Complementary vascular-protective actions of magnesium and taurine: a rationale for magnesium taurate. Med Hypotheses. 1996 Feb;46(2):89-100.8692051Kopple JD, Vinton NE, Laidlaw SA, Ament ME: Effect of intravenous taurine supplementation on plasma, blood cell, and urine taurine concentrations in adults undergoing long-term parenteral nutrition. Am J Clin Nutr. 1990 Nov;52(5):846-53.2122710McMahon GP, O'Kennedy R, Kelly MT: High-performance liquid chromatographic determination of taurine in human plasma using pre-column extraction and derivatization. J Pharm Biomed Anal. 1996 Jun;14(8-10):1287-94.8818047Stover JF, Morganti-Kosmann MC, Lenzlinger PM, Stocker R, Kempski OS, Kossmann T: Glutamate and taurine are increased in ventricular cerebrospinal fluid of severely brain-injured patients. J Neurotrauma. 1999 Feb;16(2):135-42.10098958Learn DB, Fried VA, Thomas EL: Taurine and hypotaurine content of human leukocytes. J Leukoc Biol. 1990 Aug;48(2):174-82.2370482Miglis M, Wilder D, Reid T, Bakaltcheva I: Effect of taurine on platelets and the plasma coagulation system. Platelets. 2002 Feb;13(1):5-10.11918831Axelson M, Ellis E, Mork B, Garmark K, Abrahamsson A, Bjorkhem I, Ericzon BG, Einarsson C: Bile acid synthesis in cultured human hepatocytes: support for an alternative biosynthetic pathway to cholic acid. Hepatology. 2000 Jun;31(6):1305-12.10827156Hu S, Zhao X, Yin S, Meng J: [A study on the mechanism of taurine postponing the aging process of human fetal brain neural cells] Wei Sheng Yan Jiu. 1997 Mar;26(2):98-101.10325611Goodman HO, Shihabi Z, Oles KS: Antiepileptic drugs and plasma and platelet taurine in epilepsy. Epilepsia. 1989 Mar-Apr;30(2):201-7.2494044Sturman JA, Messing JM, Rossi SS, Hofmann AF, Neuringer MD: Tissue taurine content and conjugated bile acid composition of rhesus monkey infants fed a human infant soy-protein formula with or without taurine supplementation for 3 months. Neurochem Res. 1988 Apr;13(4):311-6.3393260Gonzalez-Quevedo A, Obregon F, Santiesteban Freixas R, Fernandez R, Lima L: [Amino acids as biochemical markers in epidemic and endemic optic neuropathies] Rev Cubana Med Trop. 1998;50 Suppl:241-4.10349454Hu, Libo; Zhu, Hui; Du, Da-Ming; Xu, Jiaxi. Efficient synthesis of taurine and structurally diverse substituted taurines from aziridines. Journal of Organic Chemistry (2007), 72(12), 4543-4546.http://hmdb.ca/system/metabolites/msds/000/000/184/original/HMDB00251.pdf?1358895978Gamma-glutamyltranspeptidaseP18956GGT_ECOLIggthttp://ecmdb.ca/proteins/P18956.xmlAlpha-ketoglutarate-dependent taurine dioxygenaseP37610TAUD_ECOLItauDhttp://ecmdb.ca/proteins/P37610.xmlGlutamate decarboxylase alphaP69908DCEA_ECOLIgadAhttp://ecmdb.ca/proteins/P69908.xmlGlutamate decarboxylase betaP69910DCEB_ECOLIgadBhttp://ecmdb.ca/proteins/P69910.xmlTaurine transport system permease protein tauCQ47539TAUC_ECOLItauChttp://ecmdb.ca/proteins/Q47539.xmlTaurine import ATP-binding protein TauBQ47538TAUB_ECOLItauBhttp://ecmdb.ca/proteins/Q47538.xmlTaurine-binding periplasmic proteinQ47537TAUA_ECOLItauAhttp://ecmdb.ca/proteins/Q47537.xmlProline/betaine transporterP0C0L7PROP_ECOLIproPhttp://ecmdb.ca/proteins/P0C0L7.xmlTaurine transport system permease protein tauCQ47539TAUC_ECOLItauChttp://ecmdb.ca/proteins/Q47539.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlTaurine import ATP-binding protein TauBQ47538TAUB_ECOLItauBhttp://ecmdb.ca/proteins/Q47538.xmlTaurine-binding periplasmic proteinQ47537TAUA_ECOLItauAhttp://ecmdb.ca/proteins/Q47537.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlAdenosine triphosphate + Water + Taurine > ADP + Hydrogen ion + Phosphate + TaurineABC-64-RXNAdenosine triphosphate + Water + Taurine > ADP + Hydrogen ion + Phosphate + TaurineABC-64-RXNalpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acidR05320Cysteic acid <> Taurine + Carbon dioxideR01682(5-L-Glutamyl)-peptide + Taurine <> Peptide + 5-L-Glutamyl-taurineR01687Taurine + alpha-Ketoglutarate + Oxygen <> Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxideR05320Taurine + Adenosine triphosphate + Water > Taurine + ADP + Phosphate + Hydrogen ionABC-64-RXNTaurine + Adenosine triphosphate + Water > Taurine + ADP + Phosphate + Hydrogen ionABC-64-RXNTaurine + Oxoglutaric acid + Oxygen > Hydrogen ion + Aminoacetaldehyde + Sulfite + Succinic acid + Carbon dioxideRXN0-299Adenosine triphosphate + Water + Taurine > ADP + Inorganic phosphate + TaurineAdenosine triphosphate + Water + Taurine > ADP + Inorganic phosphate + TaurineTaurine + Oxoglutaric acid + Oxygen > Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxideADP + Phosphate + 4 Hydrogen ion + Heme + Nickel(2+) + Iron chelate + Taurine + Molybdate + Magnesium + Fe3+ + Potassium + Polyamine + vitamin B12 + Sulfate + glycerol-3-phosphate + Phosphonate + D-Maltose <> Adenosine triphosphate +3 Hydrogen ion + WaterR00086RXN0-1061Cysteic acid + Cysteic acid > Taurine + Carbon dioxidePW_R002556Taurine + (5-L-Glutamyl)-peptide > 5-L-Glutamyl-taurine + PeptidePW_R002557Taurine + Oxoglutaric acid + Oxygen > Sulfite + Succinic acid + Aminoacetaldehyde + Carbon dioxide + SulfitePW_R002558Taurine + Oxoglutaric acid + Oxygen > Sulfite + Succinic acid + Carbon dioxide + Hydrogen ion + Aminoacetaldehyde + SulfitePW_R003461Taurine + Adenosine triphosphate + Water > Taurine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADPPW_RCT000166Taurine + Adenosine triphosphate + Water > Taurine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADPPW_RCT000166alpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acidTaurine + alpha-Ketoglutarate + Oxygen <> Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxidealpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acid