2.02012-05-31 13:45:41 -06002015-09-13 12:56:10 -0600ECMDB01123M2MDB0002622-Aminobenzoic acid2-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-carboxybenzene2-Amino-Benzoate2-Amino-Benzoic acid2-Aminobenzoate2-Aminobenzoic acid2-Aminophenylacetate2-Aminophenylacetic acid2-CarboxyanilineAnthranateAnthranic acidAnthranilateAnthranilate grAnthranilic acidAnthranilic acid grCarboxyanilineH-2-Abz-OHKyselina anthranilovaKyselina O-aminobenzoovaO-Amino-BenzoateO-Amino-Benzoic acidO-AminobenzoateO-Aminobenzoic acidO-AnthranilateO-Anthranilic acidO-CarboxyanilineOrtho-amidobenzoateOrtho-amidobenzoic acidOrtho-aminobenzoateOrtho-aminobenzoic acidVitamin LVitamin L1C7H7NO2137.136137.0476784732-aminobenzoic acid2-aminobenzoic acid118-92-3NC1=CC=CC=C1C(O)=OInChI=1S/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10)RWZYAGGXGHYGMB-UHFFFAOYSA-NSolidCytosollogp0.78logs-1.30solubility6.81e+00 g/lmelting_point146.5 oClogp1.45pka_strongest_acidic4.89pka_strongest_basic1.95iupac2-aminobenzoic acidaverage_mass137.136mono_mass137.047678473smilesNC1=CC=CC=C1C(O)=OformulaC7H7NO2inchiInChI=1S/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10)inchikeyRWZYAGGXGHYGMB-UHFFFAOYSA-Npolar_surface_area63.32refractivity38.01polarizability13.29rotatable_bond_count1acceptor_count3donor_count2physiological_charge-1formal_charge0Phenylalanine, tyrosine and tryptophan biosynthesisec00400Tryptophan metabolismThe 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
PW000815ec00380MetabolicBiphenyl degradationec006211,4-Dichlorobenzene degradationec00627Microbial metabolism in diverse environmentsec01120Metabolic pathwayseco01100tryptophan metabolism IIThe 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-CoAPW001916Metabolictryptophan biosynthesisTRPSYN-PWYSpecdb::CMs865Specdb::CMs866Specdb::CMs867Specdb::CMs1180Specdb::CMs1297Specdb::CMs2604Specdb::CMs26997Specdb::CMs30062Specdb::CMs30175Specdb::CMs30480Specdb::CMs30823Specdb::CMs31277Specdb::CMs31278Specdb::CMs37934Specdb::CMs130719Specdb::CMs138453Specdb::EiMs321Specdb::NmrOneD1646Specdb::NmrOneD2175Specdb::NmrOneD4822Specdb::NmrOneD8682Specdb::NmrOneD8683Specdb::NmrOneD8684Specdb::NmrOneD8685Specdb::NmrOneD8686Specdb::NmrOneD8687Specdb::NmrOneD8688Specdb::NmrOneD8689Specdb::NmrOneD8690Specdb::NmrOneD8691Specdb::NmrOneD8692Specdb::NmrOneD8693Specdb::NmrOneD8694Specdb::NmrOneD8695Specdb::NmrOneD8696Specdb::NmrOneD8697Specdb::NmrOneD8698Specdb::NmrOneD8699Specdb::NmrOneD8700Specdb::NmrOneD8701Specdb::NmrOneD166595Specdb::MsMs6270Specdb::MsMs6271Specdb::MsMs6272Specdb::MsMs6273Specdb::MsMs6274Specdb::MsMs6275Specdb::MsMs6276Specdb::MsMs6277Specdb::MsMs6278Specdb::MsMs6279Specdb::MsMs6280Specdb::MsMs6281Specdb::MsMs6282Specdb::MsMs6283Specdb::MsMs6284Specdb::MsMs6285Specdb::MsMs6286Specdb::MsMs6287Specdb::MsMs6288Specdb::MsMs6292Specdb::MsMs6293Specdb::MsMs20297Specdb::MsMs20298Specdb::MsMs20299Specdb::MsMs21848Specdb::NmrTwoD1053Specdb::NmrTwoD1587HMDB01123227222C0010830754ANTHRANILATEBE2Anthranilic acidKeseler, I. 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Huaxue Shijie (1999), 40(5), 274-277. http://hmdb.ca/system/metabolites/msds/000/001/010/original/HMDB01123.pdf?1358463404Anthranilate synthase component 1P00895TRPE_ECOLItrpEhttp://ecmdb.ca/proteins/P00895.xmlAnthranilate synthase component IIP00904TRPG_ECOLItrpDhttp://ecmdb.ca/proteins/P00904.xmlN-hydroxyarylamine O-acetyltransferaseP77567NHOA_ECOLInhoAhttp://ecmdb.ca/proteins/P77567.xmlChorismate + L-Glutamine <> 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidR00986ANTHRANSYN-RXN2-Aminobenzoic acid + Phosphoribosyl pyrophosphate > Pyrophosphate + N-(5-Phospho-D-ribosyl)anthranilateR01073PRTRANS-RXNAcetyl-CoA + 2-Aminobenzoic acid > N-Acetylanthranilate + Coenzyme AChorismate + Ammonia <> 2-Aminobenzoic acid + Pyruvic acid + WaterR00985Chorismate + L-Glutamine <> 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateR00986N-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate <> 2-Aminobenzoic acid + Phosphoribosyl pyrophosphateR01073Chorismate + L-Glutamine > Hydrogen ion + 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateR00986ANTHRANSYN-RXNN-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate < 2-Aminobenzoic acid + Phosphoribosyl pyrophosphatePRTRANS-RXNHydrogen ion + methyl red + NADH 2-Aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NADRXN0-5375Chorismate + L-Glutamine > 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateN-(5-Phospho-D-ribosyl)anthranilate + Pyrophosphate > 2-Aminobenzoic acid + Phosphoribosyl pyrophosphateChorismate + L-Glutamine > L-Glutamic acid + Pyruvic acid + Hydrogen ion + 2-Aminobenzoic acid + L-GlutamatePW_R0028942-Aminobenzoic acid + Phosphoribosyl pyrophosphate > Pyrophosphate + N-(5-phosphoribosyl)-anthranilate + N-(5-phosphoribosyl)-anthranilatePW_R002895Chorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidChorismate + Ammonia <>2 2-Aminobenzoic acid + Pyruvic acid + WaterChorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidChorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidGutnick 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 glucoseShake flask and filter culture3.48uM0.037 oCK12 NCM3722Mid-Log Phase139200Bennett, 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 5:593-599.19561621Gutnick 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 glycerolShake flask and filter culture2.66uM0.037 oCK12 NCM3722Mid-Log Phase106400Bennett, 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 5:593-599.19561621Gutnick 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 acetateShake flask and filter culture3.44uM0.037 oCK12 NCM3722Mid-Log Phase137600Bennett, 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 5:593-599.1956162148 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 GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h5.07uM0.037 oCBW25113Stationary Phase, glucose limited202800Ishii, 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