2.0 2015-09-08 17:50:01 -0600 2015-09-14 16:46:31 -0600 ECMDB24195 M2MDB006312 γ-L-glutamyl 5-phosphate gamma-L-Glutamyl 5-phosphate is an intermediate in L-proline biosynthesis I pathway in E.coli. It is a product for the enzyme gamma-glutamyl kinase which catalyzes the reaction L-glutamate + ATP -> gamma-L-glutamyl 5-phosphate + ADP. It is also the substrate for the enzyme glutamate-5-semialdehyde dehydrogenase which catalyzes the reaction gamma-L-glutamyl 5-phosphate + NADPH + H+ -> L-glutamate-5-semialdehyde + NADP+ + phosphate (BioCyc compound: L-GLUTAMATE-5-P). γ-L-glutamyl 5-phosphoric acid C5H8NO7P 225.094 225.004935759 (2S)-2-amino-5-(hydrogen phosphonatooxy)-5-oxopentanoate (2S)-2-amino-5-(hydrogen phosphonatooxy)-5-oxopentanoate [H][C@](N)(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)/p-2/t3-/m0/s1 PJRXVIJAERNUIP-VKHMYHEASA-L logp -1.46 ALOGPS logs -0.84 ALOGPS solubility 3.82e+01 g/l ALOGPS logp -3 ChemAxon pka_strongest_acidic 1.12 ChemAxon pka_strongest_basic 9.51 ChemAxon iupac (2S)-2-amino-5-(hydrogen phosphonatooxy)-5-oxopentanoate ChemAxon average_mass 225.094 ChemAxon mono_mass 225.004935759 ChemAxon smiles [H][C@](N)(CCC(=O)OP(O)([O-])=O)C([O-])=O ChemAxon formula C5H8NO7P 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)/p-2/t3-/m0/s1 ChemAxon inchikey PJRXVIJAERNUIP-VKHMYHEASA-L ChemAxon polar_surface_area 152.81 ChemAxon refractivity 52.16 ChemAxon polarizability 17.28 ChemAxon rotatable_bond_count 6 ChemAxon acceptor_count 7 ChemAxon donor_count 2 ChemAxon physiological_charge -2 ChemAxon formal_charge -2 ChemAxon 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 Specdb::NmrOneD 335818 Specdb::NmrOneD 335819 Specdb::NmrOneD 335820 Specdb::NmrOneD 335821 Specdb::NmrOneD 335822 Specdb::NmrOneD 335823 Specdb::NmrOneD 335824 Specdb::NmrOneD 335825 Specdb::NmrOneD 335826 Specdb::NmrOneD 335827 Specdb::NmrOneD 335828 Specdb::NmrOneD 335829 Specdb::NmrOneD 335830 Specdb::NmrOneD 335831 Specdb::NmrOneD 335832 Specdb::NmrOneD 335833 Specdb::NmrOneD 335834 Specdb::NmrOneD 335835 Specdb::NmrOneD 335836 Specdb::NmrOneD 335837 Specdb::MsMs 29591 Specdb::MsMs 29592 Specdb::MsMs 29593 Specdb::MsMs 36149 Specdb::MsMs 36150 Specdb::MsMs 36151 Glutamate 5-kinase P0A7B5 PROB_ECOLI proB http://ecmdb.ca/proteins/P0A7B5.xml L-Glutamic acid + Adenosine triphosphate + L-Glutamate > Adenosine diphosphate + γ-L-glutamyl 5-phosphate + ADP PW_R002715