2.0 2012-05-31 14:02:20 -0600 2015-06-03 15:54:37 -0600 ECMDB04017 M2MDB000561 gamma-Aminobutyric acid Gamma-aminobutyric acid (GABA) is a metabolite of glutamate. Gamma-aminobutyric acid was first synthesized in 1883, and was first known only as a plant and microbial metabolic product. In 1950, however, GABA was discovered to be an integral part of the mammalian central nervous system. Organisms synthesize GABA from glutamate using the enzyme L-glutamic acid decarboxylase and pyridoxal phosphate (which is the active form of vitamin B6) as a cofactor. (Wikipedia) &gamma;-amino-N-butyrate &gamma;-amino-n-butyric acid &gamma;-aminobutyrate &gamma;-aminobutyric acid 3-Carboxypropylamine 4-AB 4-amino-<i>n</i>-butyric acid 4-Amino-N-butyrate 4-Amino-N-butyric acid 4-Aminobutanoate 4-Aminobutanoic acid 4-Aminobutyrate 4-Aminobutyric acid 4-NH2-but 4-NH3-but Aminalon g Aminobutyrate g Aminobutyric acid G-Amino-N-butyrate G-Amino-N-butyric acid g-Aminobutyrate g-Aminobutyric acid GABA Gaballon Gamarex Gamma Aminobutyrate Gamma Aminobutyric acid Gamma-Amino-N-butyrate Gamma-Amino-N-butyric acid Gamma-Aminobutyrate Gamma-Aminobutyric acid Gammalon Gammalone Gammar Gammasol Mielogen Mielomade Omega-Aminobutyrate Omega-Aminobutyric acid Piperidate Piperidic acid Piperidinate Piperidinic acid W-Aminobutyrate W-Aminobutyric acid γ Aminobutyrate γ Aminobutyric acid γ-amino-N-Butyrate γ-amino-N-Butyric acid γ-Aminobutyrate γ-Aminobutyric acid C4H9NO2 103.1198 103.063328537 4-aminobutanoic acid gamma(amino)-butyric acid 56-12-2 NCCCC(O)=O InChI=1S/C4H9NO2/c5-3-1-2-4(6)7/h1-3,5H2,(H,6,7) BTCSSZJGUNDROE-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm logp -2.99 ALOGPS logs 0.55 ALOGPS solubility 3.65e+02 g/l ALOGPS melting_point 203 oC logp -2.9 ChemAxon pka_strongest_acidic 4.53 ChemAxon pka_strongest_basic 10.22 ChemAxon iupac 4-aminobutanoic acid ChemAxon average_mass 103.1198 ChemAxon mono_mass 103.063328537 ChemAxon smiles NCCCC(O)=O ChemAxon formula C4H9NO2 ChemAxon inchi InChI=1S/C4H9NO2/c5-3-1-2-4(6)7/h1-3,5H2,(H,6,7) ChemAxon inchikey BTCSSZJGUNDROE-UHFFFAOYSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 25.46 ChemAxon polarizability 10.62 ChemAxon rotatable_bond_count 3 ChemAxon acceptor_count 3 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Butanoate metabolism ec00650 Alanine, aspartate and glutamate metabolism ec00250 Arginine and proline metabolism ec00330 beta-Alanine metabolism The Beta-Alanine Metabolism starts with a product of Aspartate metabolism. Aspartate is decarboxylated by aspartate 1-decarboxylase, releasing carbon dioxide and Beta-alanine. Beta alanine is then metabolized through a pantothenate synthetase resulting in Pantothenic acid undergoes phosphorylation through a ATP driven pantothenate kinase, resulting in D-4-phosphopantothenate. Pantothenate (vitamin B5) is the universal precursor for the synthesis of the 4'-phosphopantetheine moiety of coenzyme A and acyl carrier protein. Only plants and microorganismscan synthesize pantothenate de novo - animals require a dietary supplement. The enzymes of this pathway are therefore considered to be antimicrobial drug targets. PW000896 ec00410 Metabolic 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 Valine, leucine and isoleucine degradation ec00280 Metabolic pathways eco01100 arginine metabolism The metabolism of L-arginine starts with the acetylation of L-glutamic acid resulting in a N-acetylglutamic acid while releasing a coenzyme A and a hydrogen ion. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NDPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. L-glutamine is used to synthesize carbamoyl phosphate through the interaction of L-glutamine, water, ATP, and hydrogen carbonate. This reaction yields ADP, L-glutamic acid, phosphate, and hydrogen ion. Carbamoyl phosphate and ornithine are used to catalyze the production of citrulline through an ornithine carbamoyltransferase. Citrulline reacts with L-aspartic acid through an ATP dependent enzyme, argininosuccinate synthase to produce pyrophosphate, AMP and argininosuccinic acid. Argininosussinic acid is then lyase to produce L-arginine and fumaric acid. L-arginine can be metabolized into succinic acid by two different sets of reactions: 1. Arginine reacts with succinyl-CoA through a arginine N-succinyltransferase resulting in N2-succinyl-L-arginine while releasing CoA and Hydrogen Ion. N2-succinyl-L-arginine is then dihydrolase to produce a N2-succinyl-L-ornithine through a N-succinylarginine dihydrolase. This compound in turn reacts with oxoglutaric acid through succinylornithine transaminase resulting in L-glutamic acid and N2-succinyl-L-glutamic acid 5-semialdehyde. This compoud in turn reacts with a NAD dependent dehydrogenase resulting in N2-succinylglutamate while releasing NADH and hydrogen ion. N2-succinylglutamate reacts with water through a succinylglutamate desuccinylase resulting in L-glutamic acid and a succinic acid. The succinic acid is then incorporated in the TCA cycle 2.Argine reacts with carbon dioxide and a hydrogen ion through a biodegradative arginine decarboxylase, resulting in Agmatine. This compound is then transformed into putrescine by reacting with water and an agmatinase, and releasing urea. Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid. Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. L-arginine is eventua lly metabolized into succinic acid which then goes to the TCA cycle PW000790 Metabolic ornithine metabolism In the ornithine biosynthesis pathway of E. coli, L-glutamate is acetylated to N-acetylglutamate by the enzyme N-acetylglutamate synthase, encoded by the argA gene. The acetyl donor for this reaction is acetyl-CoA. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NADPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. Ornithine interacts with hydrogen ion through a Ornithine decarboxylase resulting in a carbon dioxide release and a putrescine Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid. Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. PW000791 Metabolic 4-aminobutanoate degradation I E. coli can utilize putrescine as the sole source of carbon and nitrogen. The enzymes of the putrescine degradation II pathway are inducible by extracellular putrescine, leading to the production of GABA. Both enzymes of this pathway are inducible by putrescine in E. coli. This variant of the pathway includes a 2-oxoglutarate-dependent 4-aminobutyrate transaminase and an NAD+-dependent dehydrogenase. This combination of enzymes has been documented in bacteria and animals and in some plants. Regarding the hydrogenase, NAD-specific variants have been studied from many bacteria, plant and animals. PW002068 Metabolic Putrescine Degradation II Several metabolic pathways for putrescine degradation as a source of nitrogen for E. coli K-12 are known. The first putrescine degradation pathway was found in in 1985. That pathway is dedicated to the degradation of intracellular putrescine. A second pathway was found in E. coli K-12 twenty years later. This pathway seems to be dedicated to the degradation of extracellular putrescine. The pathway was discovered following the discovery of a cluster of seven unassigned genes on the E. coli K-12 chromosome. In addition to a putrescine transporter, encoded by the puuP gene, the cluster contains four genes that encode the enzymes involved in this pathway, and two additional genes (puuE and puuR) that encode an enzyme involved in the catabolism of GABA (see superpathway of 4-aminobutanoate degradation) and a regulator. In this pathway, putrescine is γ-glutamylated at the expense of an ATP molecule. The resulting γ-glutamyl-putrescine is oxidized to γ-glutamyl-γ-aminobutyraldehyde, which is then dehydrogenated into 4-(glutamylamino) butanoate. In the last step, the γ-glutamyl group is removed by hydrolysis, generating 4-aminobutyrate. The key difference between this pathway and putrescine degradation I is the γ-glutamylation of putrescine. In the other pathway, putrescine is degraded directly to 4-amino-butanal. Wild type E. coli cells are unable to utilize putrescine as the sole source of carbon at temperatures above 30°C. It is possible to select for mutants that possess this ability; these mutants contain elevated levels of the enzymes in this pathway. (EcoCyc) PW002054 Metabolic 4-aminobutyrate degradation I PWY-6535 4-aminobutyrate degradation II PWY-6537 putrescine degradation I PUTDEG-PWY putrescine degradation II PWY0-1221 glutamate dependent acid resistance PWY0-1305 Specdb::CMs 324 Specdb::CMs 325 Specdb::CMs 326 Specdb::CMs 327 Specdb::CMs 328 Specdb::CMs 329 Specdb::CMs 330 Specdb::CMs 1035 Specdb::CMs 1214 Specdb::CMs 2943 Specdb::CMs 29921 Specdb::CMs 30067 Specdb::CMs 30167 Specdb::CMs 30243 Specdb::CMs 30254 Specdb::CMs 30255 Specdb::CMs 30256 Specdb::CMs 30451 Specdb::CMs 30916 Specdb::CMs 31000 Specdb::CMs 31001 Specdb::CMs 32293 Specdb::CMs 32294 Specdb::CMs 32295 Specdb::CMs 37298 Specdb::EiMs 1137 Specdb::NmrOneD 1088 Specdb::NmrOneD 1150 Specdb::NmrOneD 2464 Specdb::NmrOneD 3156 Specdb::NmrOneD 4849 Specdb::NmrOneD 5712 Specdb::NmrOneD 5713 Specdb::NmrOneD 5714 Specdb::NmrOneD 5715 Specdb::NmrOneD 5716 Specdb::NmrOneD 5717 Specdb::NmrOneD 5718 Specdb::NmrOneD 5719 Specdb::NmrOneD 5720 Specdb::NmrOneD 5721 Specdb::NmrOneD 5722 Specdb::NmrOneD 5723 Specdb::NmrOneD 5724 Specdb::NmrOneD 5725 Specdb::NmrOneD 5726 Specdb::NmrOneD 5727 Specdb::NmrOneD 5728 Specdb::NmrOneD 5729 Specdb::NmrOneD 5730 Specdb::NmrOneD 5731 Specdb::MsMs 162 Specdb::MsMs 163 Specdb::MsMs 164 Specdb::MsMs 2874 Specdb::MsMs 2875 Specdb::MsMs 2876 Specdb::MsMs 2877 Specdb::MsMs 2878 Specdb::MsMs 2879 Specdb::MsMs 2880 Specdb::MsMs 2881 Specdb::MsMs 2882 Specdb::MsMs 2883 Specdb::MsMs 2884 Specdb::MsMs 2885 Specdb::MsMs 2886 Specdb::MsMs 2887 Specdb::MsMs 2888 Specdb::MsMs 2889 Specdb::MsMs 2897 Specdb::MsMs 20672 Specdb::MsMs 20673 Specdb::MsMs 20674 Specdb::MsMs 20690 Specdb::MsMs 20691 Specdb::NmrTwoD 1146 HMDB00112 119 116 C00334 16865 4-AMINO-BUTYRATE ABU GABA 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 Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. 18402659 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 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776 Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. 12097436 Zarnowska ED, Pearce RA, Saad AA, Perouansky M: The gamma-subunit governs the susceptibility of recombinant gamma-aminobutyric acid type A receptors to block by the nonimmobilizer 1,2-dichlorohexafluorocyclobutane (F6, 2N). Anesth Analg. 2005 Aug;101(2):401-6, table of contents. 16037152 Levy LM, Levy-Reis I, Fujii M, Dalakas MC: Brain gamma-aminobutyric acid changes in stiff-person syndrome. Arch Neurol. 2005 Jun;62(6):970-4. 15956168 Hasler G, Neumeister A, van der Veen JW, Tumonis T, Bain EE, Shen J, Drevets WC, Charney DS: Normal prefrontal gamma-aminobutyric acid levels in remitted depressed subjects determined by proton magnetic resonance spectroscopy. Biol Psychiatry. 2005 Dec 15;58(12):969-73. Epub 2005 Jul 25. 16043137 Denda M, Inoue K, Inomata S, Denda S: gamma-Aminobutyric acid (A) receptor agonists accelerate cutaneous barrier recovery and prevent epidermal hyperplasia induced by barrier disruption. J Invest Dermatol. 2002 Nov;119(5):1041-7. 12445190 Wiens SC, Trudeau VL: Thyroid hormone and gamma-aminobutyric acid (GABA) interactions in neuroendocrine systems. Comp Biochem Physiol A Mol Integr Physiol. 2006 Jul;144(3):332-44. Epub 2006 Mar 9. 16527506 Choi C, Coupland NJ, Hanstock CC, Ogilvie CJ, Higgins AC, Gheorghiu D, Allen PS: Brain gamma-aminobutyric acid measurement by proton double-quantum filtering with selective J rewinding. Magn Reson Med. 2005 Aug;54(2):272-9. 16032672 Metzeler K, Agoston A, Gratzl M: An Intrinsic gamma-aminobutyric acid (GABA)ergic system in the adrenal cortex: findings from human and rat adrenal glands and the NCI-H295R cell line. Endocrinology. 2004 May;145(5):2402-11. Epub 2004 Jan 15. 14726441 Naini AB, Vontzalidou E, Cote LJ: Isocratic HPLC assay with electrochemical detection of free gamma-aminobutyric acid in cerebrospinal fluid. Clin Chem. 1993 Feb;39(2):247-50. 8432013 Levy LM, Henkin RI: Brain gamma-aminobutyric acid levels are decreased in patients with phantageusia and phantosmia demonstrated by magnetic resonance spectroscopy. J Comput Assist Tomogr. 2004 Nov-Dec;28(6):721-7. 15538143 Rating D, Siemes H, Loscher W: Low CSF GABA concentration in children with febrile convulsions, untreated epilepsy, and meningitis. J Neurol. 1983;230(4):217-25. 6198481 Spanaki MV, Siegel H, Kopylev L, Fazilat S, Dean A, Liow K, Ben-Menachem E, Gaillard WD, Theodore WH: The effect of vigabatrin (gamma-vinyl GABA) on cerebral blood flow and metabolism. Neurology. 1999 Oct 22;53(7):1518-22. 10534261 Campollo O, MacGillivray BB, McIntyre N: [Association of plasma ammonia and GABA levels and the degree of hepatic encephalopathy] Rev Invest Clin. 1992 Oct-Dec;44(4):483-90. 1485027 Nicholson-Guthrie CS, Guthrie GD, Sutton GP, Baenziger JC: Urine GABA levels in ovarian cancer patients: elevated GABA in malignancy. Cancer Lett. 2001 Jan 10;162(1):27-30. 11121859 Nisijima K, Ishiguro T: Cerebrospinal fluid levels of monoamine metabolites and gamma-aminobutyric acid in neuroleptic malignant syndrome. J Psychiatr Res. 1995 May-Jun;29(3):233-44. 7473299 Minoshima, Ryoichi. Preparation of gamma-aminobutyric acid with unripened beans. PCT Int. Appl. (2007), 25pp. 4-aminobutyrate aminotransferase P22256 GABT_ECOLI gabT http://ecmdb.ca/proteins/P22256.xml 4-aminobutyrate aminotransferase_ P50457 PUUE_ECOLI puuE http://ecmdb.ca/proteins/P50457.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 Gamma-glutamyl-gamma-aminobutyrate hydrolase P76038 PUUD_ECOLI puuD http://ecmdb.ca/proteins/P76038.xml Gamma-aminobutyraldehyde dehydrogenase P77674 ABDH_ECOLI ydcW http://ecmdb.ca/proteins/P77674.xml GABA permease P25527 GABP_ECOLI gabP http://ecmdb.ca/proteins/P25527.xml Probable glutamate/gamma-aminobutyrate antiporter P63235 GADC_ECOLI gadC http://ecmdb.ca/proteins/P63235.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 Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml gamma-Aminobutyric acid + alpha-Ketoglutarate <> L-Glutamate + Succinic acid semialdehyde R01648 L-Glutamate + Hydrogen ion <> gamma-Aminobutyric acid + Carbon dioxide R00261 GLUTDECARBOX-RXN 4-(Glutamylamino) butanoate + Water <> gamma-Aminobutyric acid + L-Glutamate R07419 RXN0-3942 4-Aminobutyraldehyde + Water + NAD <> gamma-Aminobutyric acid +2 Hydrogen ion + NADH R02549 AMINOBUTDEHYDROG-RXN L-Glutamate <> gamma-Aminobutyric acid + Carbon dioxide R00261 4-Aminobutyraldehyde + NAD + Water <> gamma-Aminobutyric acid + NADH + Hydrogen ion R02549 4-Aminobutyraldehyde + NAD + Water > gamma-Aminobutyric acid + NADH + Hydrogen ion AMINOBUTDEHYDROG-RXN Oxoglutaric acid + gamma-Aminobutyric acid <> L-Glutamate + Succinic acid semialdehyde GABATRANSAM-RXN Hydrogen ion + L-Glutamate > Carbon dioxide + gamma-Aminobutyric acid GLUTDECARBOX-RXN 4-(Glutamylamino) butanoate + Water > gamma-Aminobutyric acid + L-Glutamate RXN0-3942 4-Aminobutyraldehyde + NAD + Water > gamma-Aminobutyric acid + NADH L-Glutamate > gamma-Aminobutyric acid + Carbon dioxide gamma-Aminobutyric acid + Oxoglutaric acid > Succinic acid semialdehyde + L-Glutamate GABATRANSAM-RXN 4-(Glutamylamino) butanoate + Water > L-Glutamic acid + gamma-Aminobutyric acid + L-Glutamate PW_R002688 gamma-Aminobutyric acid + Oxoglutaric acid > Succinic acid semialdehyde + L-Glutamic acid + L-Glutamate PW_R002691 gamma-glutamyl-gamma-aminobutyrate + Water > gamma-Aminobutyric acid + L-Glutamate PW_R006001 gamma-Aminobutyric acid + alpha-Ketoglutarate <> L-Glutamate + Succinic acid semialdehyde gamma-Aminobutyric acid + alpha-Ketoglutarate <> L-Glutamate + Succinic acid semialdehyde 48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 43.6 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 174400 0 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776