2.0 2012-05-31 10:24:56 -0600 2015-09-13 12:56:07 -0600 ECMDB00251 M2MDB000106 Taurine Taurine 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-sulfonate 1-Aminoethane-2-sulfonic acid 1-Aminoethane-2-sulphonate 1-Aminoethane-2-sulphonic acid 2-Aminoethanesulfonate 2-Aminoethanesulfonic acid 2-Aminoethanesulphonate 2-Aminoethanesulphonic acid 2-Aminoethylsulfonate 2-Aminoethylsulfonic acid 2-Aminoethylsulphonate 2-Aminoethylsulphonic acid 2-Sulfoethylamine 2-Sulphoethylamine Aminoethylsulfonate Aminoethylsulfonic acid Aminoethylsulphonate Aminoethylsulphonic acid Aminoetylsulfonate Aminoetylsulfonic acid Aminoetylsulphonate Aminoetylsulphonic acid B-Aminoethylsulfonate B-Aminoethylsulfonic acid B-Aminoethylsulphonate B-Aminoethylsulphonic acid Beta-Aminoethylsulfonate Beta-Aminoethylsulfonic acid Beta-Aminoethylsulphonate Beta-Aminoethylsulphonic acid Ethylaminesulfonate Ethylaminesulfonic acid Ethylaminesulphonate Ethylaminesulphonic acid Taufon Tauphon Taurine β-Aminoethylsulfonate β-Aminoethylsulfonic acid β-Aminoethylsulphonate β-Aminoethylsulphonic acid C2H7NO3S 125.147 125.014663785 2-aminoethane-1-sulfonic acid taurine 107-35-7 NCCS(O)(=O)=O InChI=1S/C2H7NO3S/c3-1-2-7(4,5)6/h1-3H2,(H,4,5,6) XOAAWQZATWQOTB-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm logp -2.19 ALOGPS logs -0.08 ALOGPS solubility 1.05e+02 g/l ALOGPS melting_point 300 oC logp -2.6 ChemAxon pka_strongest_acidic -1.5 ChemAxon pka_strongest_basic 9.34 ChemAxon iupac 2-aminoethane-1-sulfonic acid ChemAxon average_mass 125.147 ChemAxon mono_mass 125.014663785 ChemAxon smiles NCCS(O)(=O)=O ChemAxon formula C2H7NO3S ChemAxon inchi InChI=1S/C2H7NO3S/c3-1-2-7(4,5)6/h1-3H2,(H,4,5,6) ChemAxon inchikey XOAAWQZATWQOTB-UHFFFAOYSA-N ChemAxon polar_surface_area 80.39 ChemAxon refractivity 24.61 ChemAxon polarizability 10.82 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Sulfur metabolism 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 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. PW000922 ec00920 Metabolic Taurine and hypotaurine metabolism ec00430 ABC transporters ec02010 Taurine 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 dioxide PW000774 Metabolic Taurine 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 dioxide PW001028 Metabolic inner membrane transport list 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 added PW000786 Metabolic sulfur 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. PW000923 Metabolic sulfur 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. PW000925 Metabolic sulfur 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. PW000926 Metabolic sulfur 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. PW000927 Metabolic sulfur 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. PW000924 Metabolic taurine degradation IV PWY0-981 Specdb::CMs 487 Specdb::CMs 488 Specdb::CMs 489 Specdb::CMs 2519 Specdb::CMs 30234 Specdb::CMs 30698 Specdb::CMs 30763 Specdb::CMs 32381 Specdb::CMs 32383 Specdb::CMs 166328 Specdb::EiMs 1313 Specdb::NmrOneD 1218 Specdb::NmrOneD 1277 Specdb::NmrOneD 2107 Specdb::NmrOneD 4964 Specdb::NmrOneD 6272 Specdb::NmrOneD 6273 Specdb::NmrOneD 6274 Specdb::NmrOneD 6275 Specdb::NmrOneD 6276 Specdb::NmrOneD 6277 Specdb::NmrOneD 6278 Specdb::NmrOneD 6279 Specdb::NmrOneD 6280 Specdb::NmrOneD 6281 Specdb::NmrOneD 6282 Specdb::NmrOneD 6283 Specdb::NmrOneD 6284 Specdb::NmrOneD 6285 Specdb::NmrOneD 6286 Specdb::NmrOneD 6287 Specdb::NmrOneD 6288 Specdb::NmrOneD 6289 Specdb::NmrOneD 6290 Specdb::NmrOneD 6291 Specdb::NmrOneD 166456 Specdb::MsMs 430 Specdb::MsMs 431 Specdb::MsMs 432 Specdb::MsMs 3742 Specdb::MsMs 3743 Specdb::MsMs 3744 Specdb::MsMs 3745 Specdb::MsMs 3746 Specdb::MsMs 3747 Specdb::MsMs 3748 Specdb::MsMs 3749 Specdb::MsMs 3750 Specdb::MsMs 3751 Specdb::MsMs 3752 Specdb::MsMs 3753 Specdb::MsMs 3754 Specdb::MsMs 3755 Specdb::MsMs 3756 Specdb::MsMs 3757 Specdb::MsMs 3758 Specdb::MsMs 3759 Specdb::MsMs 3760 Specdb::MsMs 3761 Specdb::MsMs 3762 Specdb::MsMs 3763 Specdb::NmrTwoD 1007 Specdb::NmrTwoD 1238 HMDB00251 1123 1091 C00245 15891 TAURINE TAU Taurine 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 Sreekumar 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. 19212411 Engelborghs 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. 12834252 Hagenfeldt 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. 6198473 Peng 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. 15911239 Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. 12297216 Rainesalo 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. 14992292 Khan 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. 15780050 Vinton 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. 3106924 Gonzalez-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. 11842876 Schneider 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. 16923232 McCarty MF: Complementary vascular-protective actions of magnesium and taurine: a rationale for magnesium taurate. Med Hypotheses. 1996 Feb;46(2):89-100. 8692051 Kopple 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. 2122710 McMahon 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. 8818047 Stover 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. 10098958 Learn DB, Fried VA, Thomas EL: Taurine and hypotaurine content of human leukocytes. J Leukoc Biol. 1990 Aug;48(2):174-82. 2370482 Miglis M, Wilder D, Reid T, Bakaltcheva I: Effect of taurine on platelets and the plasma coagulation system. Platelets. 2002 Feb;13(1):5-10. 11918831 Axelson 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. 10827156 Hu 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. 10325611 Goodman HO, Shihabi Z, Oles KS: Antiepileptic drugs and plasma and platelet taurine in epilepsy. Epilepsia. 1989 Mar-Apr;30(2):201-7. 2494044 Sturman 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. 3393260 Gonzalez-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. 10349454 Hu, 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?1358895978 Gamma-glutamyltranspeptidase P18956 GGT_ECOLI ggt http://ecmdb.ca/proteins/P18956.xml Alpha-ketoglutarate-dependent taurine dioxygenase P37610 TAUD_ECOLI tauD http://ecmdb.ca/proteins/P37610.xml Glutamate decarboxylase alpha P69908 DCEA_ECOLI gadA http://ecmdb.ca/proteins/P69908.xml Glutamate decarboxylase beta P69910 DCEB_ECOLI gadB http://ecmdb.ca/proteins/P69910.xml Taurine transport system permease protein tauC Q47539 TAUC_ECOLI tauC http://ecmdb.ca/proteins/Q47539.xml Taurine import ATP-binding protein TauB Q47538 TAUB_ECOLI tauB http://ecmdb.ca/proteins/Q47538.xml Taurine-binding periplasmic protein Q47537 TAUA_ECOLI tauA http://ecmdb.ca/proteins/Q47537.xml Proline/betaine transporter P0C0L7 PROP_ECOLI proP http://ecmdb.ca/proteins/P0C0L7.xml Taurine transport system permease protein tauC Q47539 TAUC_ECOLI tauC http://ecmdb.ca/proteins/Q47539.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Taurine import ATP-binding protein TauB Q47538 TAUB_ECOLI tauB http://ecmdb.ca/proteins/Q47538.xml Taurine-binding periplasmic protein Q47537 TAUA_ECOLI tauA http://ecmdb.ca/proteins/Q47537.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Adenosine triphosphate + Water + Taurine > ADP + Hydrogen ion + Phosphate + Taurine ABC-64-RXN Adenosine triphosphate + Water + Taurine > ADP + Hydrogen ion + Phosphate + Taurine ABC-64-RXN alpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acid R05320 Cysteic acid <> Taurine + Carbon dioxide R01682 (5-L-Glutamyl)-peptide + Taurine <> Peptide + 5-L-Glutamyl-taurine R01687 Taurine + alpha-Ketoglutarate + Oxygen <> Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxide R05320 Taurine + Adenosine triphosphate + Water > Taurine + ADP + Phosphate + Hydrogen ion ABC-64-RXN Taurine + Adenosine triphosphate + Water > Taurine + ADP + Phosphate + Hydrogen ion ABC-64-RXN Taurine + Oxoglutaric acid + Oxygen > Hydrogen ion + Aminoacetaldehyde + Sulfite + Succinic acid + Carbon dioxide RXN0-299 Adenosine triphosphate + Water + Taurine > ADP + Inorganic phosphate + Taurine Adenosine triphosphate + Water + Taurine > ADP + Inorganic phosphate + Taurine Taurine + Oxoglutaric acid + Oxygen > Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxide ADP + 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 + Water R00086 RXN0-1061 Cysteic acid + Cysteic acid > Taurine + Carbon dioxide PW_R002556 Taurine + (5-L-Glutamyl)-peptide > 5-L-Glutamyl-taurine + Peptide PW_R002557 Taurine + Oxoglutaric acid + Oxygen > Sulfite + Succinic acid + Aminoacetaldehyde + Carbon dioxide + Sulfite PW_R002558 Taurine + Oxoglutaric acid + Oxygen > Sulfite + Succinic acid + Carbon dioxide + Hydrogen ion + Aminoacetaldehyde + Sulfite PW_R003461 Taurine + Adenosine triphosphate + Water > Taurine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADP PW_RCT000166 Taurine + Adenosine triphosphate + Water > Taurine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADP PW_RCT000166 alpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acid Taurine + alpha-Ketoglutarate + Oxygen <> Sulfite + Aminoacetaldehyde + Succinic acid + Carbon dioxide alpha-Ketoglutarate + Oxygen + Taurine <> Aminoacetaldehyde + Carbon dioxide + Hydrogen ion + Sulfite + Succinic acid