2.02012-05-31 10:23:39 -06002015-09-13 12:56:06 -0600ECMDB00205M2MDB000084Phenylpyruvic acidPhenylpyruvic acid is a keto-acid that is an intermediate or catabolic byproduct of phenylalanine metabolism. It has a slight honey-like odor. Phenylalanine is converted to phenylpyruvic acid. In particular, excessive phenylalanine can be metabolized into phenylketones through, a transaminase pathway route involving glutamate. Metabolites of this transamination reaction include phenylacetate, phenylpyruvate and phenethylamine.α-ketohydrocinnamateα-ketohydrocinnamic acid2-Keto-phenyl-pyruvate2-Keto-phenyl-pyruvic acid2-Oxo-3-phenylpropanoate2-Oxo-3-phenylpropanoic acid3-Phenyl-2-oxopropanoate3-Phenyl-2-oxopropanoic acid3-Phenylpyruvate3-Phenylpyruvic acida-Ketohydrocinnamatea-Ketohydrocinnamic acidAlpha-KetohydrocinnamateAlpha-Ketohydrocinnamic acidB-PhenylpyruvateB-Phenylpyruvic acidBeta-PhenylpyruvateBeta-Phenylpyruvic acidKeto-PhenylpyruvateKeto-Phenylpyruvic acidPhenylpyroracematePhenylpyroracemic acidPhenylpyruvateα-Ketohydrocinnamateα-Ketohydrocinnamic acidβ-Phenylpyruvateβ-Phenylpyruvic acidC9H8O3164.158164.0473441222-oxo-3-phenylpropanoic acidphenylpyruvic acid156-06-9OC(=O)C(=O)CC1=CC=CC=C1InChI=1S/C9H8O3/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5H,6H2,(H,11,12)BTNMPGBKDVTSJY-UHFFFAOYSA-NSolidCytosolmelting_point154logp1.9pka_strongest_acidic3.33pka_strongest_basic-9.8iupac2-oxo-3-phenylpropanoic acidaverage_mass164.158mono_mass164.047344122smilesOC(=O)C(=O)CC1=CC=CC=C1formulaC9H8O3inchiInChI=1S/C9H8O3/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5H,6H2,(H,11,12)inchikeyBTNMPGBKDVTSJY-UHFFFAOYSA-Npolar_surface_area54.37refractivity42.71polarizability15.75rotatable_bond_count3acceptor_count3donor_count1physiological_charge-1formal_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 biosynthesisec00400phenylalanine 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 tyrosinePW000807Metabolicphenylalanine biosynthesis IPHESYNSpecdb::CMs458Specdb::CMs459Specdb::CMs460Specdb::CMs461Specdb::CMs462Specdb::CMs1216Specdb::CMs1278Specdb::CMs1383Specdb::CMs2776Specdb::CMs30240Specdb::CMs30915Specdb::CMs31068Specdb::CMs31069Specdb::CMs31070Specdb::CMs31618Specdb::CMs31619Specdb::CMs31620Specdb::CMs32188Specdb::CMs37354Specdb::CMs152691Specdb::CMs1054026Specdb::CMs1054028Specdb::CMs1054029Specdb::EiMs1076Specdb::NmrOneD1185Specdb::NmrOneD166333Specdb::NmrOneD166677Specdb::MsMs328Specdb::MsMs329Specdb::MsMs330Specdb::MsMs178839Specdb::MsMs178840Specdb::MsMs178841Specdb::MsMs181161Specdb::MsMs181162Specdb::MsMs181163Specdb::MsMs1471169Specdb::MsMs1471190Specdb::MsMs2234598Specdb::MsMs2327649Specdb::MsMs2327650Specdb::MsMs2327651Specdb::MsMs2634527Specdb::MsMs2634528Specdb::MsMs2634529Specdb::NmrTwoD1204HMDB00205997972C0016618005PHENYL-PYRUVATEPPYKeseler, I. 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Faming Zhuanli Shenqing Gongkai Shuomingshu (1996), 5 pp. http://hmdb.ca/system/metabolites/msds/000/000/143/original/HMDB00205.pdf?1358462482Aspartate aminotransferaseP00509AAT_ECOLIaspChttp://ecmdb.ca/proteins/P00509.xmlAromatic-amino-acid aminotransferaseP04693TYRB_ECOLItyrBhttp://ecmdb.ca/proteins/P04693.xmlHistidinol-phosphate aminotransferaseP06986HIS8_ECOLIhisChttp://ecmdb.ca/proteins/P06986.xmlD-amino acid dehydrogenase small subunitP0A6J5DADA_ECOLIdadAhttp://ecmdb.ca/proteins/P0A6J5.xmlP-proteinP0A9J8PHEA_ECOLIpheAhttp://ecmdb.ca/proteins/P0A9J8.xmlBranched-chain-amino-acid aminotransferaseP0AB80ILVE_ECOLIilvEhttp://ecmdb.ca/proteins/P0AB80.xmlalpha-Ketoglutarate + L-Phenylalanine <> L-Glutamate + Phenylpyruvic acidR00694Hydrogen ion + Prephenate > Carbon dioxide + Water + Phenylpyruvic acidR01373PREPHENATEDEHYDRAT-RXNPrephenate <> Phenylpyruvic acid + Water + Carbon dioxideR01373D-Phenylalanine + Water + Acceptor <> Phenylpyruvic acid + Ammonia + Reduced acceptorR01374Phenylpyruvic acid + L-Glutamate <> L-Phenylalanine + Oxoglutaric acidPHEAMINOTRANS-RXNPrephenate > Phenylpyruvic acid + Water + Carbon dioxidePhenylpyruvic acid + Ammonia + cytochrome c nitrite reductase <> D-Phenylalanine + Water + cytochrome c nitrite reductasePW_R003457Phenylpyruvic acid + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Phenylalanine + L-PhenylalaninePW_R002861L-Phenylalanine + Oxygen + L-Phenylalanine <> Oxoglutaric acid + Phenylpyruvic acidPW_R003456alpha-Ketoglutarate + L-Phenylalanine <> L-Glutamate + Phenylpyruvic acidHydrogen ion + Prephenate > Carbon dioxide + Water + Phenylpyruvic acidalpha-Ketoglutarate + L-Phenylalanine <> L-Glutamate + Phenylpyruvic acidalpha-Ketoglutarate + L-Phenylalanine <> L-Glutamate + Phenylpyruvic 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 culture89.8uM0.037 oCK12 NCM3722Mid-Log Phase3592000Bennett, 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 culture195.0uM0.037 oCK12 NCM3722Mid-Log Phase7800000Bennett, 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 culture148.0uM0.037 oCK12 NCM3722Mid-Log Phase5920000Bennett, 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