2.0 2012-05-31 13:45:41 -0600 2015-09-13 12:56:10 -0600 ECMDB01123 M2MDB000262 2-Aminobenzoic acid 2-Aminobenzoic acid is an organic compound. It is a substrate of enzyme anthranilate hydroxylase [EC 1.14.13.35] in benzoate degradation via hydroxylation pathway (KEGG). 1-Amino-2-carboxybenzene 2-Amino-Benzoate 2-Amino-Benzoic acid 2-Aminobenzoate 2-Aminobenzoic acid 2-Aminophenylacetate 2-Aminophenylacetic acid 2-Carboxyaniline Anthranate Anthranic acid Anthranilate Anthranilate gr Anthranilic acid Anthranilic acid gr Carboxyaniline H-2-Abz-OH Kyselina anthranilova Kyselina O-aminobenzoova O-Amino-Benzoate O-Amino-Benzoic acid O-Aminobenzoate O-Aminobenzoic acid O-Anthranilate O-Anthranilic acid O-Carboxyaniline Ortho-amidobenzoate Ortho-amidobenzoic acid Ortho-aminobenzoate Ortho-aminobenzoic acid Vitamin L Vitamin L1 C7H7NO2 137.136 137.047678473 2-aminobenzoic acid 2-aminobenzoic acid 118-92-3 NC1=CC=CC=C1C(O)=O InChI=1S/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10) RWZYAGGXGHYGMB-UHFFFAOYSA-N Solid Cytosol logp 0.78 ALOGPS logs -1.30 ALOGPS solubility 6.81e+00 g/l ALOGPS melting_point 146.5 oC logp 1.45 ChemAxon pka_strongest_acidic 4.89 ChemAxon pka_strongest_basic 1.95 ChemAxon iupac 2-aminobenzoic acid ChemAxon average_mass 137.136 ChemAxon mono_mass 137.047678473 ChemAxon smiles NC1=CC=CC=C1C(O)=O ChemAxon formula C7H7NO2 ChemAxon inchi InChI=1S/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10) ChemAxon inchikey RWZYAGGXGHYGMB-UHFFFAOYSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 38.01 ChemAxon polarizability 13.29 ChemAxon rotatable_bond_count 1 ChemAxon acceptor_count 3 ChemAxon donor_count 2 ChemAxon physiological_charge -1 ChemAxon formal_charge 0 ChemAxon Phenylalanine, tyrosine and tryptophan biosynthesis ec00400 Tryptophan metabolism The biosynthesis of L-tryptophan begins with L-glutamine interacting with a chorismate through a anthranilate synthase which results in a L-glutamic acid, a pyruvic acid, a hydrogen ion and a 2-aminobenzoic acid. The aminobenzoic acid interacts with a phosphoribosyl pyrophosphate through an anthranilate synthase component II resulting in a pyrophosphate and a N-(5-phosphoribosyl)-anthranilate. The latter compound is then metabolized by an indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in a 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate. This compound then interacts with a hydrogen ion through a indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in the release of carbon dioxide, a water molecule and a (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate. The latter compound then interacts with a D-glyceraldehyde 3-phosphate and an Indole. The indole interacts with an L-serine through a tryptophan synthase, β subunit dimer resulting in a water molecule and an L-tryptophan. The metabolism of L-tryptophan starts with L-tryptophan being dehydrogenated by a tryptophanase / L-cysteine desulfhydrase resulting in the release of a hydrogen ion, an Indole and a 2-aminoacrylic acid. The latter compound is isomerized into a 2-iminopropanoate. This compound then interacts with a water molecule and a hydrogen ion spontaneously resulting in the release of an Ammonium and a pyruvic acid. The pyruvic acid then interacts with a coenzyme A through a NAD driven pyruvate dehydrogenase complex resulting in the release of a NADH, a carbon dioxide and an Acetyl-CoA PW000815 ec00380 Metabolic Biphenyl degradation ec00621 1,4-Dichlorobenzene degradation ec00627 Microbial metabolism in diverse environments ec01120 Metabolic pathways eco01100 tryptophan metabolism II The biosynthesis of L-tryptophan begins with L-glutamine interacting with a chorismate through a anthranilate synthase which results in a L-glutamic acid, a pyruvic acid, a hydrogen ion and a 2-aminobenzoic acid. The aminobenzoic acid interacts with a phosphoribosyl pyrophosphate through an anthranilate synthase component II resulting in a pyrophosphate and a N-(5-phosphoribosyl)-anthranilate. The latter compound is then metabolized by an indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in a 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate. This compound then interacts with a hydrogen ion through a indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in the release of carbon dioxide, a water molecule and a (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate. The latter compound then interacts with a D-glyceraldehyde 3-phosphate and an Indole. The indole interacts with an L-serine through a tryptophan synthase, β subunit dimer resulting in a water molecule and an L-tryptophan. The metabolism of L-tryptophan starts with L-tryptophan being dehydrogenated by a tryptophanase / L-cysteine desulfhydrase resulting in the release of a hydrogen ion, an Indole and a 2-aminoacrylic acid. The latter compound is isomerized into a 2-iminopropanoate. This compound then interacts with a water molecule and a hydrogen ion spontaneously resulting in the release of an Ammonium and a pyruvic acid. The pyruvic acid then interacts with a coenzyme A through a NAD driven pyruvate dehydrogenase complex resulting in the release of a NADH, a carbon dioxide and an Acetyl-CoA PW001916 Metabolic tryptophan biosynthesis TRPSYN-PWY Specdb::CMs 865 Specdb::CMs 866 Specdb::CMs 867 Specdb::CMs 1180 Specdb::CMs 1297 Specdb::CMs 2604 Specdb::CMs 26997 Specdb::CMs 30062 Specdb::CMs 30175 Specdb::CMs 30480 Specdb::CMs 30823 Specdb::CMs 31277 Specdb::CMs 31278 Specdb::CMs 37934 Specdb::CMs 130719 Specdb::CMs 138453 Specdb::EiMs 321 Specdb::NmrOneD 1646 Specdb::NmrOneD 2175 Specdb::NmrOneD 4822 Specdb::NmrOneD 8682 Specdb::NmrOneD 8683 Specdb::NmrOneD 8684 Specdb::NmrOneD 8685 Specdb::NmrOneD 8686 Specdb::NmrOneD 8687 Specdb::NmrOneD 8688 Specdb::NmrOneD 8689 Specdb::NmrOneD 8690 Specdb::NmrOneD 8691 Specdb::NmrOneD 8692 Specdb::NmrOneD 8693 Specdb::NmrOneD 8694 Specdb::NmrOneD 8695 Specdb::NmrOneD 8696 Specdb::NmrOneD 8697 Specdb::NmrOneD 8698 Specdb::NmrOneD 8699 Specdb::NmrOneD 8700 Specdb::NmrOneD 8701 Specdb::NmrOneD 166595 Specdb::MsMs 6270 Specdb::MsMs 6271 Specdb::MsMs 6272 Specdb::MsMs 6273 Specdb::MsMs 6274 Specdb::MsMs 6275 Specdb::MsMs 6276 Specdb::MsMs 6277 Specdb::MsMs 6278 Specdb::MsMs 6279 Specdb::MsMs 6280 Specdb::MsMs 6281 Specdb::MsMs 6282 Specdb::MsMs 6283 Specdb::MsMs 6284 Specdb::MsMs 6285 Specdb::MsMs 6286 Specdb::MsMs 6287 Specdb::MsMs 6288 Specdb::MsMs 6292 Specdb::MsMs 6293 Specdb::MsMs 20297 Specdb::MsMs 20298 Specdb::MsMs 20299 Specdb::MsMs 21848 Specdb::NmrTwoD 1053 Specdb::NmrTwoD 1587 HMDB01123 227 222 C00108 30754 ANTHRANILATE BE2 Anthranilic acid Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. 21097882 Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. 17765195 Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. 18331064 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 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 Igari T, Tsuchizawa M, Shimamura T: Alteration of tryptophan metabolism in the synovial fluid of patients with rheumatoid arthritis and osteoarthritis. Tohoku J Exp Med. 1987 Oct;153(2):79-86. 3500530 Calandra P: Research on tryptophan metabolites &quot;via kynurenine&quot; in epidermis of man and mouse. Acta Vitaminol Enzymol. 1975;29(1-6):158-60. 1244085 Di Marco GS, Quinto BM, Juliano M, Carmona AK, Stella RC, Plavnik FL, Casarini DE: Purification and characterization of a neutral endopeptidase-like enzyme from human urine. J Hypertens. 1998 Dec;16(12 Pt 2):1971-8. 9886885 Hagag N, Birnbaum ER, Darnall DW: Resonance energy transfer between cysteine-34, tryptophan-214, and tyrosine-411 of human serum albumin. Biochemistry. 1983 May 10;22(10):2420-7. 6860638 Little CH, Georgiou GM, Shelton MJ, Simpson F, Cone RE: Clinical and immunological responses in subjects sensitive to solvents. Arch Environ Health. 1999 Jan-Feb;54(1):6-14. 10025410 Ritchie MR, Morton MS, Thompson AM, Deighton N, Blake A, Cummings JH, Steel CM: Investigation of the reliability of 24 h urine excretion as a biomarker of isoflavone exposure over time and over a wide range of isoflavone intakes. Eur J Clin Nutr. 2004 Sep;58(9):1286-9. 15054404 Ortega RM, Andres P, Martinez RM, Lopez-Sobaler AM: Vitamin A status during the third trimester of pregnancy in Spanish women: influence on concentrations of vitamin A in breast milk. Am J Clin Nutr. 1997 Sep;66(3):564-8. 9280174 Alves MF, Araujo MC, Juliano MA, Oliveira EM, Krieger JE, Casarini DE, Juliano L, Carmona AK: A continuous fluorescent assay for the determination of plasma and tissue angiotensin I-converting enzyme activity. Braz J Med Biol Res. 2005 Jun;38(6):861-8. Epub 2005 Jun 1. 15933779 Soma J, Sugawara T, Huang YD, Nakajima J, Kawamura M: Tranilast slows the progression of advanced diabetic nephropathy. Nephron. 2002;92(3):693-8. 12372957 Ahmad S: The functional roles of cytochrome P-450 mediated systems: present knowledge and future areas of investigations. Drug Metab Rev. 1979;10(1):1-14. 118858 Spivak W, Carey MC: Reverse-phase h.p.l.c. separation, quantification and preparation of bilirubin and its conjugates from native bile. Quantitative analysis of the intact tetrapyrroles based on h.p.l.c. of their ethyl anthranilate azo derivatives. Biochem J. 1985 Feb 1;225(3):787-805. 3919713 Wang, Chengyin; Yang, Jisheng; Wang, Honghai. Production of o-aminobenzoic acid from by-product o-nitrobenzoic acid. Huaxue Shijie (1999), 40(5), 274-277. http://hmdb.ca/system/metabolites/msds/000/001/010/original/HMDB01123.pdf?1358463404 Anthranilate synthase component 1 P00895 TRPE_ECOLI trpE http://ecmdb.ca/proteins/P00895.xml Anthranilate synthase component II P00904 TRPG_ECOLI trpD http://ecmdb.ca/proteins/P00904.xml N-hydroxyarylamine O-acetyltransferase P77567 NHOA_ECOLI nhoA http://ecmdb.ca/proteins/P77567.xml Chorismate + L-Glutamine <> 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acid R00986 ANTHRANSYN-RXN 2-Aminobenzoic acid + Phosphoribosyl pyrophosphate > Pyrophosphate + N-(5-Phospho-D-ribosyl)anthranilate R01073 PRTRANS-RXN Acetyl-CoA + 2-Aminobenzoic acid > N-Acetylanthranilate + Coenzyme A Chorismate + Ammonia <> 2-Aminobenzoic acid + Pyruvic acid + Water R00985 Chorismate + L-Glutamine <> 2-Aminobenzoic acid + Pyruvic acid + L-Glutamate R00986 N-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate <> 2-Aminobenzoic acid + Phosphoribosyl pyrophosphate R01073 Chorismate + L-Glutamine > Hydrogen ion + 2-Aminobenzoic acid + Pyruvic acid + L-Glutamate R00986 ANTHRANSYN-RXN N-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate < 2-Aminobenzoic acid + Phosphoribosyl pyrophosphate PRTRANS-RXN Hydrogen ion + methyl red + NADH 2-Aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD RXN0-5375 Chorismate + L-Glutamine > 2-Aminobenzoic acid + Pyruvic acid + L-Glutamate N-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate > 2-Aminobenzoic acid + Phosphoribosyl pyrophosphate Chorismate + L-Glutamine > L-Glutamic acid + Pyruvic acid + Hydrogen ion + 2-Aminobenzoic acid + L-Glutamate PW_R002894 2-Aminobenzoic acid + Phosphoribosyl pyrophosphate > Pyrophosphate + N-(5-phosphoribosyl)-anthranilate + N-(5-phosphoribosyl)-anthranilate PW_R002895 Chorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acid Chorismate + Ammonia <>2 2-Aminobenzoic acid + Pyruvic acid + Water Chorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acid Chorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acid Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucose Shake flask and filter culture 3.48 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 13920 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerol Shake flask and filter culture 2.66 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 10640 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetate Shake flask and filter culture 3.44 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 13760 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 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 5.07 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 20280 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