2.0 2012-05-31 13:48:00 -0600 2015-06-03 15:53:51 -0600 ECMDB01228 M2MDB000304 L-Glutamic acid 5-phosphate L-Glutamic acid 5-phosphate is an intermediate in the urea cycle and metabolism of amino groups, a substrate of aldehyde dehydrogenase 18 family, member A1 [EC:2.7.2.11 1.2.1.41] (KEGG) Glu-5-P L-&gamma;-glutamyl-5-P L-&gamma;-glutamyl-5-phosphate L-&gamma;-glutamyl-5-phosphoric acid L-g-Glutamyl-5-P L-g-Glutamyl-5-phosphate L-g-Glutamyl-5-phosphoric acid L-gamma-Glutamyl-5-P L-gamma-Glutamyl-5-phosphate L-gamma-Glutamyl-5-phosphoric acid L-Glutamate 5-phosphate L-Glutamate-5-phosphate L-Glutamic acid 5-phosphate L-Glutamic acid 5-phosphoric acid L-Glutamic acid-5-phosphoric acid L-Glutamyl 5-phosphate L-Glutamyl 5-phosphoric acid L-Glutamyl-5-P L-Glutamyl-5-phosphate L-Glutamyl-5-phosphoric acid L-γ-Glutamyl-5-P L-γ-Glutamyl-5-phosphate L-γ-Glutamyl-5-phosphoric acid C5H10NO7P 227.1092 227.019488191 (2S)-2-amino-5-oxo-5-(phosphonooxy)pentanoic acid L-gamma-glutamyl phosphate 13254-53-0 N[C@@H](CCC(=O)OP(O)(O)=O)C(O)=O InChI=1S/C5H10NO7P/c6-3(5(8)9)1-2-4(7)13-14(10,11)12/h3H,1-2,6H2,(H,8,9)(H2,10,11,12)/t3-/m0/s1 PJRXVIJAERNUIP-VKHMYHEASA-N Solid Cytosol logp -1.96 ALOGPS logs -1.32 ALOGPS solubility 1.09e+01 g/l ALOGPS logp -3 ChemAxon pka_strongest_acidic 1.12 ChemAxon pka_strongest_basic 9.51 ChemAxon iupac (2S)-2-amino-5-oxo-5-(phosphonooxy)pentanoic acid ChemAxon average_mass 227.1092 ChemAxon mono_mass 227.019488191 ChemAxon smiles N[C@@H](CCC(=O)OP(O)(O)=O)C(O)=O ChemAxon formula C5H10NO7P ChemAxon inchi InChI=1S/C5H10NO7P/c6-3(5(8)9)1-2-4(7)13-14(10,11)12/h3H,1-2,6H2,(H,8,9)(H2,10,11,12)/t3-/m0/s1 ChemAxon inchikey PJRXVIJAERNUIP-VKHMYHEASA-N ChemAxon polar_surface_area 147.15 ChemAxon refractivity 42.45 ChemAxon polarizability 18.09 ChemAxon rotatable_bond_count 6 ChemAxon acceptor_count 7 ChemAxon donor_count 4 ChemAxon physiological_charge -2 ChemAxon formal_charge 0 ChemAxon Arginine and proline metabolism ec00330 Metabolic pathways eco01100 proline metabolism The biosynthesis of L-proline in E. coli involves L-glutamic acid being phosphorylated through an ATP driven glutamate 5-kinase resulting in a L-glutamic acid 5-phosphate. This compound is then reduced through a NADPH driven gamma glutamyl phosphate reductase resulting in the release of a phosphate, a NADP and a L-glutamic gamma-semialdehyde. L-glutamic gamma-semialdehyde is dehydrated spontaneously, resulting in a release of water,hydrogen ion and 1-Pyrroline-5-carboxylic acid. The latter compound is reduced by an NADPH driven pyrroline-5-carboxylate reductase which is subsequently reduced to L-proline. L-proline works as a repressor of the pyrroline-5-carboxylate reductase enzyme and glutamate 5-kinase. In E. coli, the biosynthesis of L-proline from L-glutamate is governed by three genetic loci namely proB, proA and proC. The first reaction in the pathway is catalyzed by γ-glutamyl kinase, encoded by proB . The second reaction, NADPH-dependent reduction of γ-glutamyl phosphate to glutamate-5-semialdehyde, in the pathway is catalyzed by glutamate-5-semialdehyde dehydrogenase, encoded by proA . These two enzymes aggregate into a multimeric bi-functional enzyme complex known as γ-glutamyl kinase-GP-reductase multienzyme complex. It is believed that the complex formation serves to protect the highly labile glutamyl phosphate from the hostile nucleophilic and aqueous environment found in the cell . The final step in the pathway, the reduction of pyrroline 5-carboxylate to L-proline, is catalyzed by an NADPH-dependent pyrroline-5-carboxylate reductase encoded by proC . Proline is metabolized by being converted back to L-glutamate, which is further degraded to α-ketoglutarate, an intermediate of the TCA cycle. Curiously, L-glutamate, the obligate intermediate of the proline degradation pathway, cannot itself serve as a total source of carbon and energy for E. coli, because glutamate transport supplies exogenous glutamate at an inadequate rate. The proces by which proline is turned into L-glutamate starts with L-proline interacting with ubiquinone through a bifunctional protein putA resulting in an ubiquinol, a hydrogen ion and a 1-pyrroline-5-carboxylic acid. The latter compound is then hydrated spontaneously resulting in a L-glutamic gamma-semialdehyde. This compound is then processed by interacting with water through an NAD driven bifunctional protein putA resulting in a hydrogen ion, NADH and L-glutamic acid. PW000794 Metabolic proline biosynthesis I PROSYN-PWY Specdb::CMs 3258 Specdb::CMs 37983 Specdb::CMs 134135 Specdb::CMs 141869 Specdb::NmrOneD 87592 Specdb::NmrOneD 87593 Specdb::NmrOneD 87594 Specdb::NmrOneD 87595 Specdb::NmrOneD 87596 Specdb::NmrOneD 87597 Specdb::NmrOneD 87598 Specdb::NmrOneD 87599 Specdb::NmrOneD 87600 Specdb::NmrOneD 87601 Specdb::NmrOneD 87602 Specdb::NmrOneD 87603 Specdb::NmrOneD 87604 Specdb::NmrOneD 87605 Specdb::NmrOneD 87606 Specdb::NmrOneD 87607 Specdb::NmrOneD 87608 Specdb::NmrOneD 87609 Specdb::NmrOneD 87610 Specdb::NmrOneD 87611 Specdb::MsMs 29441 Specdb::MsMs 29442 Specdb::MsMs 29443 Specdb::MsMs 35999 Specdb::MsMs 36000 Specdb::MsMs 36001 Specdb::MsMs 2404523 Specdb::MsMs 2404524 Specdb::MsMs 2404525 Specdb::MsMs 2535063 Specdb::MsMs 2535064 Specdb::MsMs 2535065 HMDB01228 193475 167893 C03287 L-GLUTAMATE-5-P 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 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 Journal of Heterocyclic Chemistry (1987), 24(1), 279-82. Gamma-glutamyl phosphate reductase P07004 PROA_ECOLI proA http://ecmdb.ca/proteins/P07004.xml Glutamate 5-kinase P0A7B5 PROB_ECOLI proB http://ecmdb.ca/proteins/P0A7B5.xml Adenosine triphosphate + L-Glutamate > ADP + L-Glutamic acid 5-phosphate GLUTKIN-RXN L-Glutamic acid 5-phosphate + Hydrogen ion + NADPH > L-Glutamic-gamma-semialdehyde + NADP + Phosphate GLUTSEMIALDEHYDROG-RXN L-Glutamic-gamma-semialdehyde + Phosphate + NADP < L-Glutamic acid 5-phosphate + NADPH + Hydrogen ion GLUTSEMIALDEHYDROG-RXN L-Glutamic-gamma-semialdehyde + Inorganic phosphate + NADP > L-Glutamic acid 5-phosphate + NADPH Adenosine triphosphate + L-Glutamate <> ADP + L-Glutamyl 5-phosphate + L-Glutamic acid 5-phosphate R00239 L-Glutamic-gamma-semialdehyde + Phosphate + NADP <> L-Glutamyl 5-phosphate + NADPH + Hydrogen ion + L-Glutamic acid 5-phosphate R03313 L-Glutamic acid 5-phosphate + Hydrogen ion + NADPH + NADPH > L-Glutamic-gamma-semialdehyde + NADP + Phosphate PW_R002716 L-Glutamic-gamma-semialdehyde + Phosphate + NADP <> L-Glutamic acid 5-phosphate + NADPH + Hydrogen ion Adenosine triphosphate + L-Glutamate <> ADP + L-Glutamic acid 5-phosphate L-Glutamic-gamma-semialdehyde + Phosphate + NADP <> L-Glutamic acid 5-phosphate + NADPH + Hydrogen ion Adenosine triphosphate + L-Glutamate <> ADP + L-Glutamic acid 5-phosphate