2.0 2012-05-31 14:21:37 -0600 2015-06-03 17:19:04 -0600 ECMDB12283 M2MDB000839 Prephenate Prephenic acid, more commonly known by its anionic form prephenate, is an intermediate in the biosynthesis of the aromatic amino acids phenylalanine and tyrosine. 1-Carboxy-4-hydroxy-2,5-cyclohexadiene-1-pyruvate 1-Carboxy-4-hydroxy-2,5-cyclohexadiene-1-pyruvic acid PRE Prephenic acid C10H10O6 226.1828 226.047738052 1-(2-carboxy-2-oxoethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid prephenic acid 126-49-8 OC1C=CC(CC(=O)C(O)=O)(C=C1)C(O)=O InChI=1S/C10H10O6/c11-6-1-3-10(4-2-6,9(15)16)5-7(12)8(13)14/h1-4,6,11H,5H2,(H,13,14)(H,15,16) FPWMCUPFBRFMLH-UHFFFAOYSA-N Solid Cytosol logp -0.31 ALOGPS logs -0.80 ALOGPS solubility 3.60e+01 g/l ALOGPS logp 0.061 ChemAxon pka_strongest_acidic 2.89 ChemAxon pka_strongest_basic -2.1 ChemAxon iupac 1-(2-carboxy-2-oxoethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid ChemAxon average_mass 226.1828 ChemAxon mono_mass 226.047738052 ChemAxon smiles OC1C=CC(CC(=O)C(O)=O)(C=C1)C(O)=O ChemAxon formula C10H10O6 ChemAxon inchi InChI=1S/C10H10O6/c11-6-1-3-10(4-2-6,9(15)16)5-7(12)8(13)14/h1-4,6,11H,5H2,(H,13,14)(H,15,16) ChemAxon inchikey FPWMCUPFBRFMLH-UHFFFAOYSA-N ChemAxon polar_surface_area 111.9 ChemAxon refractivity 53.55 ChemAxon polarizability 19.73 ChemAxon rotatable_bond_count 4 ChemAxon acceptor_count 6 ChemAxon donor_count 3 ChemAxon physiological_charge -2 ChemAxon formal_charge 0 ChemAxon Phenylalanine metabolism The 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. PW000921 ec00360 Metabolic Phenylalanine, tyrosine and tryptophan biosynthesis ec00400 Novobiocin biosynthesis ec00401 Metabolic pathways eco01100 phenylalanine biosynthesis The 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 tyrosine PW000807 Metabolic tyrosine biosynthesis The 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 tyrosine PW000806 Metabolic phenylalanine biosynthesis I PHESYN tyrosine biosynthesis I TYRSYN Specdb::CMs 1780 Specdb::CMs 1784 Specdb::CMs 2746 Specdb::CMs 30672 Specdb::CMs 31565 Specdb::CMs 31566 Specdb::CMs 39899 Specdb::NmrOneD 4843 Specdb::NmrOneD 329082 Specdb::NmrOneD 329083 Specdb::NmrOneD 329084 Specdb::NmrOneD 329085 Specdb::NmrOneD 329086 Specdb::NmrOneD 329087 Specdb::NmrOneD 329088 Specdb::NmrOneD 329089 Specdb::NmrOneD 329090 Specdb::NmrOneD 329091 Specdb::NmrOneD 329092 Specdb::NmrOneD 329093 Specdb::NmrOneD 329094 Specdb::NmrOneD 329095 Specdb::NmrOneD 329096 Specdb::NmrOneD 329097 Specdb::NmrOneD 329098 Specdb::NmrOneD 329099 Specdb::NmrOneD 329100 Specdb::NmrOneD 329101 Specdb::MsMs 27053 Specdb::MsMs 27054 Specdb::MsMs 27055 Specdb::MsMs 33611 Specdb::MsMs 33612 Specdb::MsMs 33613 HMDB12283 1028 1001 C00254 29934 PREPHENATE 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 Aromatic-amino-acid aminotransferase P04693 TYRB_ECOLI tyrB http://ecmdb.ca/proteins/P04693.xml T-protein P07023 TYRA_ECOLI tyrA http://ecmdb.ca/proteins/P07023.xml P-protein P0A9J8 PHEA_ECOLI pheA http://ecmdb.ca/proteins/P0A9J8.xml Chorismate <> Prephenate R01715 CHORISMATEMUT-RXN Hydrogen ion + Prephenate > Carbon dioxide + Water + Phenylpyruvic acid R01373 PREPHENATEDEHYDRAT-RXN NAD + Prephenate > 4-Hydroxyphenylpyruvic acid + Carbon dioxide + NADH R01728 PREPHENATEDEHYDROG-RXN Prephenate <> Phenylpyruvic acid + Water + Carbon dioxide R01373 Prephenate + NAD <> 4-Hydroxyphenylpyruvic acid + Carbon dioxide + NADH + Hydrogen ion R01728 Oxalacetic acid + L-Arogenate <> L-Aspartic acid + Prephenate R01731 Chorismate > Prephenate CHORISMATEMUT-RXN Prephenate > Phenylpyruvic acid + Water + Carbon dioxide Prephenate + NAD > 4-hydroxyphenylpyruvate + Carbon dioxide + NADH Chorismate <> Prephenate Hydrogen ion + Prephenate > Carbon dioxide + Water + Phenylpyruvic acid Chorismate <> Prephenate