2.02012-05-31 14:08:40 -06002015-06-03 15:54:52 -0600ECMDB06503M2MDB000676Phenylacetyl-CoAPhenylacetyl-CoA is an intermediate in the metabolism of phenylacetic acid. Phenylacetyl-CoA is synthesized by the Phenylacetyl-CoA ligase protein paaK using the following reaction: ATP + phenylacetate + CoA = AMP + diphosphate + phenylacetyl-CoA.Phenylacetate-CoAPhenylacetic acid-CoAC29H42N7O17P3S885.667885.157073179{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-{[2-({2-[(2-phenylacetyl)sulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acidphenylacetyl-coa7532-39-0CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)CC1=CC=CC=C1InChI=1S/C29H42N7O17P3S/c1-29(2,24(40)27(41)32-9-8-19(37)31-10-11-57-20(38)12-17-6-4-3-5-7-17)14-50-56(47,48)53-55(45,46)49-13-18-23(52-54(42,43)44)22(39)28(51-18)36-16-35-21-25(30)33-15-34-26(21)36/h3-7,15-16,18,22-24,28,39-40H,8-14H2,1-2H3,(H,31,37)(H,32,41)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t18-,22-,23-,24+,28-/m1/s1ZIGIFDRJFZYEEQ-CECATXLMSA-NSolidCytosollogp-0.03logs-2.44solubility3.19e+00 g/llogp-5.1pka_strongest_acidic0.83pka_strongest_basic4.95iupac{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-{[2-({2-[(2-phenylacetyl)sulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acidaverage_mass885.667mono_mass885.157073179smilesCC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)CC1=CC=CC=C1formulaC29H42N7O17P3SinchiInChI=1S/C29H42N7O17P3S/c1-29(2,24(40)27(41)32-9-8-19(37)31-10-11-57-20(38)12-17-6-4-3-5-7-17)14-50-56(47,48)53-55(45,46)49-13-18-23(52-54(42,43)44)22(39)28(51-18)36-16-35-21-25(30)33-15-34-26(21)36/h3-7,15-16,18,22-24,28,39-40H,8-14H2,1-2H3,(H,31,37)(H,32,41)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t18-,22-,23-,24+,28-/m1/s1inchikeyZIGIFDRJFZYEEQ-CECATXLMSA-Npolar_surface_area363.63refractivity196.93polarizability79.56rotatable_bond_count22acceptor_count17donor_count9physiological_charge-4formal_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.PW000921ec00360MetabolicMicrobial metabolism in diverse environmentsec01120Phenylethylamine metabolismThe process of phenylethylamine metabolism starts with 2-phenylethylamine interacting with an oxygen molecule and a water molecule in the periplasmic space through a phenylethylamine oxidase. This reaction results in the release of a hydrogen peroxide, ammonium and phenylacetaldehyde.
Phenylacetaldehyde is introduced into the cytosol and degraded into phenylacetate by reaction with a phenylacetaldehyde dehydrogenase. This reaction involves phenylacetaldehyde interacting with NAD, and a water molecule and then resulting in the release of NADH, and 2 hydrogen ion.
Phenylacetate is then degraded. The first step involves phenylacetate interacting with an coenzyme A and an ATP driven phenylacetate-CoA ligase resulting in the release of a AMP, a diphosphate and a phenylacetyl-CoA. This resulting compound the interacts with a hydrogen ion, NADPH, and oxygen molecule through a ring 1,2-phenylacetyl-CoA epoxidase protein complex resulting in the release of a water molecule, an NADP and a 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA. This compound is then metabolized by a ring 1,2 epoxyphenylacetyl-CoA isomerase resulting in a 2-oxepin-2(3H)-ylideneacetyl-CoA. This compound is then hydrolated through a oxepin-CoA hydrolase resulting in a 3-oxo-5,6-didehydrosuberyl-CoA semialdehyde. This commpound then interacts with a water molecule and NADP driven 3-oxo-5,6-dehydrosuberyl-CoA semialadehyde dehydrogenase resulting in 2 hydrogen ions, a NADPH and a 3-oxo-5,6-didehydrosuberyl-CoA. The resulting compound interacts with a coenzyme A and a 3-oxo-5,6 dehydrosuberyl-CoA thiolase resulting in an acetyl-CoA and a 2,3-didehydroadipyl-CoA. This resulting compound is the hydrated by a 2,3-dehydroadipyl-CoA hydratas resulting in a 3-hydroxyadipyl-CoA whuch is dehydrogenated through an NAD driven 3-hydroxyadipyl-CoA dehydrogenase resulting in a NADH, a hydrogen ion and a 3-oxoadipyl-CoA. The latter compound then interacts with conezyme A through a beta-ketoadipyl-CoA thiolase resulting in an acetyl-CoA and a succinyl-CoA. The succinyl-CoA is then integrated into the TCA cycle.PW002027Metabolicphenylacetate degradation I (aerobic)PWY0-321Specdb::NmrOneD74652Specdb::NmrOneD74653Specdb::NmrOneD74654Specdb::NmrOneD74655Specdb::NmrOneD74656Specdb::NmrOneD74657Specdb::NmrOneD74658Specdb::NmrOneD74659Specdb::NmrOneD74660Specdb::NmrOneD74661Specdb::NmrOneD74662Specdb::NmrOneD74663Specdb::NmrOneD74664Specdb::NmrOneD74665Specdb::NmrOneD74666Specdb::NmrOneD74667Specdb::NmrOneD74668Specdb::NmrOneD74669Specdb::NmrOneD74670Specdb::NmrOneD74671Specdb::MsMs25358Specdb::MsMs25359Specdb::MsMs25360Specdb::MsMs31916Specdb::MsMs31917Specdb::MsMs31918Specdb::MsMs2346497Specdb::MsMs2346498Specdb::MsMs2346499Specdb::MsMs2593027Specdb::MsMs2593028Specdb::MsMs2593029HMDB06503439267145148C0058215537CPD-207FAQKeseler, 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-D590.21097882Kanehisa, 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-D114.22080510van 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 370:17-25.17765195Winder, 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 80:2939-2948.18331064Potempska A, Loo YH, Wisniewski HM: On the possible mechanism of phenylacetate neurotoxicity: inhibition of choline acetyltransferase by phenylacetyl-CoA. J Neurochem. 1984 May;42(5):1499-501.6142928Probable phenylacetic acid degradation NADH oxidoreductase paaEP76081PAAE_ECOLIpaaEhttp://ecmdb.ca/proteins/P76081.xmlPhenylacetate-coenzyme A ligaseP76085PAAK_ECOLIpaaKhttp://ecmdb.ca/proteins/P76085.xmlPhenylacetic acid degradation protein paaBP76078PAAB_ECOLIpaaBhttp://ecmdb.ca/proteins/P76078.xmlPhenylacetic acid degradation protein paaAP76077PAAA_ECOLIpaaAhttp://ecmdb.ca/proteins/P76077.xmlPhenylacetic acid degradation protein paaDP76080PAAD_ECOLIpaaDhttp://ecmdb.ca/proteins/P76080.xmlPhenylacetic acid degradation protein paaCP76079PAAC_ECOLIpaaChttp://ecmdb.ca/proteins/P76079.xmlthioesterase, most active with ring-hydroxylated phenylacetyl-coenzyme A thioestersP76084paaIhttp://ecmdb.ca/proteins/P76084.xmlHydrogen ion + NADPH + Oxygen + Phenylacetyl-CoA > Water + NADP + Ring 1,2-epoxyphenylacetyl-CoAAdenosine triphosphate + Coenzyme A + Benzeneacetic acid <> Adenosine monophosphate + Phenylacetyl-CoA + PyrophosphateR02539Phenylacetyl-CoA + Oxygen + NADPH + Hydrogen ion <> 2-(1,2-Epoxy-1,2-dihydrophenyl)acetyl-CoA + Water + NADP + 2-(1,2-Epoxy-1,2-dihydrophenyl)acetyl-CoAR09838Phenylacetyl-CoA + Water <> Benzeneacetic acid + Coenzyme AR09840Coenzyme A + phenylacetate + Adenosine triphosphate > Phenylacetyl-CoA + Pyrophosphate + Adenosine monophosphatePHENYLACETATE--COA-LIGASE-RXNPhenylacetyl-CoA + Oxygen + NADPH + Hydrogen ion > 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP + WaterRXN0-2042Phenylacetyl-CoA + NADPH + Oxygen > 2-(1,2-Epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP + WaterAdenosine triphosphate + Benzeneacetic acid + CoA > Adenosine monophosphate + Pyrophosphate + Phenylacetyl-CoABenzeneacetic acid + Adenosine triphosphate + Coenzyme A > Adenosine monophosphate + Pyrophosphate + Phenylacetyl-CoAPW_R005919Phenylacetyl-CoA + Hydrogen ion + NADPH + Oxygen > Water + NADP + 2-(1,2-Epoxy-1,2-dihydrophenyl)acetyl-CoAPW_R005920