2.02012-05-31 14:21:02 -06002015-06-03 17:19:03 -0600ECMDB12199M2MDB000828ChorismateChorismic acid, more commonly known as its anionic form chorismate, is an important biochemical intermediate in plants and microorganisms. It is a precursor for the aromatic amino acids phenylalanine and tyrosine,indole, indole derivatives and tryptophan,2,3-dihydroxybenzoic acid (DHB) used for enterobactin biosynthesis,the plant hormone salicylic acid and many alkaloids and other aromatic metabolites. -- WikipediaChorismic acidC10H10O6226.1828226.047738052(3R,4R)-3-[(1-carboxyeth-1-en-1-yl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acidchorismic acid55508-12-8O[C@@H]1C=CC(=C[C@H]1OC(=C)C(O)=O)C(O)=OInChI=1S/C10H10O6/c1-5(9(12)13)16-8-4-6(10(14)15)2-3-7(8)11/h2-4,7-8,11H,1H2,(H,12,13)(H,14,15)/t7-,8-/m1/s1WTFXTQVDAKGDEY-HTQZYQBOSA-NSolidCytosollogp0.52logs-1.41solubility8.80e+00 g/lmelting_point 140 °Clogp-0.13pka_strongest_acidic3.39pka_strongest_basic-3.4iupac(3R,4R)-3-[(1-carboxyeth-1-en-1-yl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acidaverage_mass226.1828mono_mass226.047738052smilesO[C@@H]1C=CC(=C[C@H]1OC(=C)C(O)=O)C(O)=OformulaC10H10O6inchiInChI=1S/C10H10O6/c1-5(9(12)13)16-8-4-6(10(14)15)2-3-7(8)11/h2-4,7-8,11H,1H2,(H,12,13)(H,14,15)/t7-,8-/m1/s1inchikeyWTFXTQVDAKGDEY-HTQZYQBOSA-Npolar_surface_area104.06refractivity54.31polarizability20.49rotatable_bond_count4acceptor_count6donor_count3physiological_charge-2formal_charge0Phenylalanine metabolismThe pathways of the metabolism of phenylalaline begins with the conversion of chorismate to prephenate through a P-protein (chorismate mutase:pheA). Prephenate then interacts with a hydrogen ion through the same previous enzyme resulting in a release of carbon dioxide, water and a phenolpyruvic acid. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosine.
Phenolpyruvic acid can also be obtained from a reversivle reaction with ammonia, a reduced acceptor and a D-amino acid dehydrogenase, resulting in a water, an acceptor and a D-phenylalanine, which can be then transported into the periplasmic space by aromatic amino acid exporter.
L-phenylalanine also interacts in two reversible reactions, one involved with oxygen through a catalase peroxidase resulting in a carbon dioxide and 2-phenylacetamide. The other reaction involved an interaction with oxygen through a phenylalanine aminotransferase resulting in a oxoglutaric acid and phenylpyruvic acid.
L-phenylalanine can be imported into the cytoplasm through an aromatic amino acid:H+ symporter AroP.
The compound can also be imported into the periplasmic space through a transporter: L-amino acid efflux transporter.PW000921ec00360MetabolicPhenylalanine, tyrosine and tryptophan biosynthesisec00400Folate biosynthesisThe biosynthesis of folic acid begins with a product of purine nucleotides de novo biosynthesis pathway, GTP. This compound is involved in a reaction with water through a GTP cyclohydrolase 1 protein complex, resulting in a hydrogen ion, formic acid and 7,8-dihydroneopterin 3-triphosphate. The latter compound is dephosphatased through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, hydrogen ion and 7,8-dihydroneopterin 3-phosphate. The latter compound reacts with water spontaneously resulting in the release of a phosphate and a 7,8 -dihydroneopterin. This compound reacts with a dihydroneopterin aldolase, releasing a glycoaldehyde and 6-hydroxymethyl-7,9-dihydropterin. The latter compound is phosphorylated with a ATP-driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in a (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.
Chorismate is metabolized by reacting with L-glutamine through a 4-amino-4-deoxychorismate synthase resulting in L-glutamic acid and 4-amino-4-deoxychorismate. The latter compound then reacts through an aminodeoxychorismate lyase resulting in pyruvic acid,hydrogen ion and p-aminobenzoic acid.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoic acid react through a dihydropteroate synthase resulting in pyrophosphate and 7,8-dihydropteroic acid. This compound reacts with L-glutamic acid through an ATP driven bifunctional folylpolyglutamate synthetase / dihydrofolate synthetase resulting in a 7,8-dihydrofolate monoglutamate. This compound is reduced through an NADPH mediated dihydrofolate reductase resulting in a tetrahydrofate.
This product goes on to a one carbon pool by folate pathway.
PW000908ec00790MetabolicTryptophan 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
PW000815ec00380MetabolicUbiquinone and other terpenoid-quinone biosynthesisec00130Biosynthesis of siderophore group nonribosomal peptides2,3-dihydroxybenzoate is synthesized from chorismate via isochorismate and 2,3-dihydroxy-2,3-dihydrobenzoate.
The biosynthesis of 2,3-dihydroxybenzoate starts from chorismate being synthesized into isochorismate through isochorismate synthase entC. EntC catalyzes the conversion of chorismate to isochorismate. The N-terminal isochorismate lyase domain of EntB hydrolyzes the pyruvate group of isochorismate to produce 2,3-dihydro-2,3-dihydroxybenzoate. The conversion of this latter compound to 2,3-dihydroxybenzoate is catalyzed by the EntA dehydrogenase.This compound then interacts with L-serine and ATP through enterobactin synthase protein complex resulting in the production of enterobactin. Enterobactin is exported into the periplasmic space through the enterobactin exporter entS. The compound is the export to the environment through the outer membrane protein TolC. In the environment enterobactin reacts with iron to produce Ferric enterobactin. This compound is imported into the periplasmic space through a ferric enterobactin outermembrane transport complex. The compound then enters the cytoplasm through a ferric enterobactin ABC transporter.Once inside the cytoplasm, ferric enterobactin spontaneously releases the iron ion from the enterobactin.
PW000760ec01053MetabolicMetabolic pathwayseco011002,3-dihydroxybenzoate biosynthesis2,3-dihydroxybenzoate is synthesized from chorismate via isochorismate and 2,3-dihydroxy-2,3-dihydrobenzoate. Chorismate is a key intermediate and branch point in the biosynthesis of many aromatic compounds.
The biosynthesis of 2,3-dihydroxybenzoate from chorismate is catalyzed by three enzymes EntC, EntB, and EntA. EntC catalyzes the conversion of chorismate to isochorismate. The N-terminal isochorismate lyase domain of EntB hydrolyzes the pyruvate group of isochorismate to produce 2,3-dihydro-2,3-dihydroxybenzoate. The conversion of this latter compound to 2,3-dihydroxybenzoate is catalyzed by the EntA dehydrogenase.
PW000751MetabolicChorismate biosynthesisChorismate is an intermediate in the synthesis of three amino acids: tyrosine, phenylalanine and tryptophan. In addition it is a precursor of folic acid, ubiquinone, menaquinone, and enterochelin. The first reaction in the chorismate pathway is catalyzed by three separate enzymes, all involved in the biosynthesis of Shikimic acid, each of which is subject to feedback inhibition by one of the three amino acids. However, even in the presence of all three amino acids, sufficient enzymatic activity is present to permit synthesis of the other four metabolites synthesized from chorismate because the enzyme subject to regulation by tryptophan cannot be inhibited more than 60 percent.
The biosynthesis of chorismate starts with D-Erythrose-4-phosphate getting transformed into 3-deoxy-D-arabino-heptulosonate-7-phosphate through a phospho-2-dehydro-3-deoxyheptonate aldolase. This is followed by a 3-dehydroquinate synthase converting the 3-deoxy-D-arabino-heptulosonate-7-phosphate into a 3-dehydroquinate which in turn is conveted to 3-dehydroshikimate through a 3-dehydroquinate dehydratase. A this point 3-dehydroshikimate can be turned into Shikimic acid through 2 different reactions involving Quinate/shikimate dehydrogenase and shikimate dehydrogenase 2. Shikimic acid is phosphorylated by Shikimate kinase 2 into shikimate 3-phosphate. Shikimate 3- phophate and a phosphoenolpyruvic acid are then joined through a 3-phosphoshikimate 1-carboxyvinyltransferase to produce a 5-enoylpyruvyl-shikimate 3-phosphate while releasing a phosphate. This in turns produces our final product Chorismate through a chorismate synthase. PW000816MetabolicMenaquinol biosythesisMenaquinol biosynthesis starts with chorismate being metabolized into isochorismate through a isochorismate synthase. Isochorismate then interacts with 2-oxoglutare and a hydrogen ion through a 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase resulting in the release of a carbon dioxide and a 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate. The latter compound then interacts with (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase resulting in the release of a pyruvate and a (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate. This compound is the dehydrated through a o-succinylbenzoate synthase resulting in the release of a water molecule and a 2-succinylbenzoate. This compound then interacts with a coenzyme A and an ATP through a o-succinylbenzoate CoA ligase resulting in the release of a diphosphate, a AMP and a succinylbenzoyl-CoA. The latter compound interacts with a hydrogen ion through a 1,4-dihydroxy-2-naphthoyl-CoA synthase resulting in the release of a water molecule or a 1,4-dihydroxy-2-naphthoyl-CoA. This compound then interacts with water through a 1,4-dihydroxy-2-naphthoyl-CoA thioesterase resulting in the release of a coenzyme A, a hydrogen ion and a 1,4-dihydroxy-2-naphthoate.
The 1,4-dihydroxy-2-naphthoate can interact with either farnesylfarnesylgeranyl-PP or octaprenyl diphosphate and a hydrogen ion through a 1,4-dihydroxy-2-naphthoate octaprenyltransferase resulting in a release of a carbon dioxide, a pyrophosphate and a demethylmenaquinol-8. This compound then interacts with SAM through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a hydrogen ion, a s-adenosyl-L-homocysteine and a menaquinol.PW001897MetabolicSecondary Metabolites: Ubiquinol biosynthesisThe biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate.
The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and a 2-octaprenyl-6-hydroxyphenol.
The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol.
The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.
PW000981Metabolicphenylalanine biosynthesisThe pathways of biosynthesis of phenylalaline and tyrosine are intimately connected. First step of both pathways is the conversion of chorismate to prephenate, the third step of both is the conversion of a ketoacid to the aminoacid through transamination. The two pathways differ only in the second step of their three-step reaction sequences: In the case of phenylalanine biosynthesis, a dehydratase converts prephenate to phenylpyruvate(reaction occurs slowly in the absence of enzymic activity); in the case of tyrosine biosynthesis, a dehydrogenase converts prephenate to p-hydroxyphenylpyruvate. Also in both pathways the first two steps are catalyzed by two distinc active sites on a single protein. Thus the first step of each pathway can be catalyzed by two enzyme: those associated with both the phenylalanine specific dehydratase and the tyrosine specific dehydrogenase. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosinePW000807Metabolictyrosine biosynthesisThe pathways of biosynthesis of phenylalaline and tyrosine are intimately connected. First step of both pathways is the conversion of chorismate to prephenate, the third step of both is the conversion of a ketoacid to the aminoacid through transamination. The two pathways differ only in the second step of their three-step reaction sequences: In the case of phenylalanine biosynthesi a dehydratase converts prephenate to phenylpyruvate(reaction occurs slowly in the absence of enzymic activity); in the case of tyrosine biosynthesis, a dehydrogenase converts prephenate to p-hydroxyphenylpyruvate. Also in both pathways the first two steps are catalyzed by two distinc active sites on a single protein. Thus the first step of each pathway can be catalyzed by two enzyme: those associated with both the phenylalanine specific dehydratase and the tyrosine specific dehydrogenase. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosinePW000806Metabolictryptophan 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-CoAPW001916MetabolicEnterobactin BiosynthesisEnterobactin is a catecholate siderophore produced almost exclusively by enterobacteria, although it has been reported in some Streptomyces species. It is a cyclic compound made of three units of 2,3-dihydroxybenzoylserine joined in a cyclic structure by lactone linkages (only the δ-cis isomer of the ferric chelate is biologically active). Not only the cyclic molecule, but also the biosynthetic precursor 2,3-dihydroxy-N-benzoylserine and its linear dimer and trimer condensation products are able to transport iron into enterobacteria.
Enterobactin is synthesized under iron-deficient conditions and excreted into the environment where it binds Fe(III) with high affinity and specificity. The ferrisiderophore complexes are taken up into the cell by specific transport components. Enterobactin synthesis is divided into two parts: 1) the conversion of chorismate to 2,3-dihydroxybenzoate 2) the synthesis of enterobactin from 2,3-dihydroxybenzoate and L-serine. (EcoCyc)PW002048MetabolicSecondary Metabolites: Ubiquinol biosynthesis 2The biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate. The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and a 2-octaprenyl-6-hydroxyphenol. The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol. The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.PW002036Metabolic1,4-dihydroxy-2-naphthoate biosynthesis IPWY-5837<i>p</i>-aminobenzoate biosynthesisPWY-6543phenylalanine biosynthesis IPHESYNtyrosine biosynthesis ITYRSYNtryptophan biosynthesisTRPSYN-PWYchorismate biosynthesis from 3-dehydroquinatePWY-61632,3-dihydroxybenzoate biosynthesisPWY-59014-hydroxybenzoate biosynthesis II (bacteria and fungi)PWY-5755Specdb::CMs3324Specdb::CMs39858Specdb::CMs135498Specdb::CMs143232Specdb::NmrOneD95678Specdb::NmrOneD95679Specdb::NmrOneD95680Specdb::NmrOneD95681Specdb::NmrOneD95682Specdb::NmrOneD95683Specdb::NmrOneD95684Specdb::NmrOneD95685Specdb::NmrOneD95686Specdb::NmrOneD95687Specdb::NmrOneD95688Specdb::NmrOneD95689Specdb::NmrOneD95690Specdb::NmrOneD95691Specdb::NmrOneD95692Specdb::NmrOneD95693Specdb::NmrOneD95694Specdb::NmrOneD95695Specdb::NmrOneD95696Specdb::NmrOneD95697Specdb::MsMs24497Specdb::MsMs24498Specdb::MsMs24499Specdb::MsMs31055Specdb::MsMs31056Specdb::MsMs31057Specdb::MsMs1470913Specdb::MsMs1470914Specdb::MsMs1470915Specdb::MsMs1471379Specdb::MsMs1471380Specdb::MsMs1471381Specdb::MsMs1471382Specdb::MsMs1471383Specdb::MsMs1471384Specdb::MsMs1471385Specdb::MsMs1471386Specdb::MsMs1471387Specdb::MsMs1471388Specdb::MsMs1471389Specdb::MsMs1471390Specdb::MsMs1472266Specdb::MsMs1472267Specdb::MsMs1472268Specdb::MsMs1472269HMDB121991203911542C0025117333CHORISMATEISJKeseler, I. 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"Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Anthranilate synthase component 1P00895TRPE_ECOLItrpEhttp://ecmdb.ca/proteins/P00895.xmlPara-aminobenzoate synthase glutamine amidotransferase component IIP00903PABA_ECOLIpabAhttp://ecmdb.ca/proteins/P00903.xmlAnthranilate synthase component IIP00904TRPG_ECOLItrpDhttp://ecmdb.ca/proteins/P00904.xmlPara-aminobenzoate synthase component 1P05041PABB_ECOLIpabBhttp://ecmdb.ca/proteins/P05041.xmlT-proteinP07023TYRA_ECOLItyrAhttp://ecmdb.ca/proteins/P07023.xmlP-proteinP0A9J8PHEA_ECOLIpheAhttp://ecmdb.ca/proteins/P0A9J8.xmlIsochorismate synthase entCP0AEJ2ENTC_ECOLIentChttp://ecmdb.ca/proteins/P0AEJ2.xmlChorismate synthaseP12008AROC_ECOLIaroChttp://ecmdb.ca/proteins/P12008.xmlChorismate--pyruvate lyaseP26602UBIC_ECOLIubiChttp://ecmdb.ca/proteins/P26602.xmlMenaquinone-specific isochorismate synthaseP38051MENF_ECOLImenFhttp://ecmdb.ca/proteins/P38051.xmlChorismate + L-Glutamine <> 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidR00986ANTHRANSYN-RXNChorismate <> PrephenateR01715CHORISMATEMUT-RXNChorismate + L-Glutamine <> 4-Amino-4-deoxychorismate + L-GlutamateR01716PABASYN-RXNChorismate <> IsochorismateR01717ISOCHORSYN-RXN5-O-(1-Carboxyvinyl)-3-phosphoshikimate <> Chorismate + PhosphateR01714CHORISMATE-SYNTHASE-RXNChorismate <> 4-Hydroxybenzoic acid + Pyruvic acidR01302CHORPYRLY-RXNChorismate + Ammonia <> 2-Aminobenzoic acid + Pyruvic acid + WaterR00985Chorismate + L-Glutamine <> 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateR009864-Hydroxybenzoic acid + Pyruvic acid <> ChorismateR01302Chorismate + L-Glutamine > Hydrogen ion + 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateR00986ANTHRANSYN-RXN5-O-(1-Carboxyvinyl)-3-phosphoshikimate > Phosphate + ChorismateR01714CHORISMATE-SYNTHASE-RXNChorismate > PrephenateCHORISMATEMUT-RXNChorismate > 4-Hydroxybenzoic acid + Pyruvic acidR01302CHORPYRLY-RXN5-O-(1-Carboxyvinyl)-3-phosphoshikimate > Chorismate + Inorganic phosphateChorismate > IsochorismateChorismate + L-Glutamine > 4-Amino-4-deoxychorismate + L-GlutamateChorismate + L-Glutamine > 2-Aminobenzoic acid + Pyruvic acid + L-GlutamateChorismate > isochorismate + IsochorismatePW_R002452Chorismate + L-Glutamine > L-Glutamic acid + Pyruvic acid + Hydrogen ion + 2-Aminobenzoic acid + L-GlutamatePW_R0028945-enolpyruvyl-shikimate 3-phosphate > Phosphate + ChorismatePW_R002917Chorismate + L-Glutamine > L-Glutamic acid + 4-amino-4-deoxychorismate + L-Glutamate + 4-Amino-4-deoxychorismatePW_R003403Chorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidChorismate + Ammonia <>2 2-Aminobenzoic acid + Pyruvic acid + WaterChorismate + L-Glutamine <>4 4-Amino-4-deoxychorismate + L-Glutamate5 5-O-(1-Carboxyvinyl)-3-phosphoshikimate <> Chorismate + PhosphateChorismate <> PrephenateChorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidChorismate + L-Glutamine <>2 2-Aminobenzoic acid + L-Glutamate + Hydrogen ion + Pyruvic acidChorismate + L-Glutamine <>4 4-Amino-4-deoxychorismate + L-GlutamateChorismate <> Prephenate