2.0 2012-05-31 14:23:05 -0600 2015-06-03 17:19:08 -0600 ECMDB20017 M2MDB000866 (S)-4-Amino-5-oxopentanoate (s)-4-amino-5-oxopentanoate is a member of the chemical class known as Gamma Amino Acids and Derivatives. These are amino acids having a (-NH2) group attached to the gamma carbon atom. (S)-4-amino-5-oxopentanoate (S)-4-amino-5-oxopentanoic acid GluSA L-Glutamate 1-semialdehyde L-Glutamic acid 1-semialdehyde C5H9NO3 131.1299 131.058243159 (4S)-4-amino-5-oxopentanoic acid glutamate-1-semialdehyde [H][C@](N)(CCC(O)=O)C=O InChI=1S/C5H9NO3/c6-4(3-7)1-2-5(8)9/h3-4H,1-2,6H2,(H,8,9)/t4-/m0/s1 MPUUQNGXJSEWTF-BYPYZUCNSA-N Cytosol logp -2.91 ALOGPS logs 0.04 ALOGPS solubility 1.43e+02 g/l ALOGPS logp -3.4 ChemAxon pka_strongest_acidic 4.03 ChemAxon pka_strongest_basic 8.1 ChemAxon iupac (4S)-4-amino-5-oxopentanoic acid ChemAxon average_mass 131.1299 ChemAxon mono_mass 131.058243159 ChemAxon smiles [H][C@](N)(CCC(O)=O)C=O ChemAxon formula C5H9NO3 ChemAxon inchi InChI=1S/C5H9NO3/c6-4(3-7)1-2-5(8)9/h3-4H,1-2,6H2,(H,8,9)/t4-/m0/s1 ChemAxon inchikey MPUUQNGXJSEWTF-BYPYZUCNSA-N ChemAxon polar_surface_area 80.39 ChemAxon refractivity 30.36 ChemAxon polarizability 12.44 ChemAxon rotatable_bond_count 4 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Porphyrin and chlorophyll metabolism ec00860 Metabolic pathways eco01100 Porphyrin metabolism The metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter . L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate. This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane. Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III. Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III. Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+ uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway. Uroporphyrinogen III can be processed in anaerobic or aerobic condition. Anaerobic: Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX Aerobic: Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX. The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway. PW000936 Metabolic tetrapyrrole biosynthesis I PWY-5188 Specdb::CMs 1086951 Specdb::NmrOneD 322752 Specdb::NmrOneD 322753 Specdb::NmrOneD 322754 Specdb::NmrOneD 322755 Specdb::NmrOneD 322756 Specdb::NmrOneD 322757 Specdb::NmrOneD 322758 Specdb::NmrOneD 322759 Specdb::NmrOneD 322760 Specdb::NmrOneD 322761 Specdb::NmrOneD 322762 Specdb::NmrOneD 322763 Specdb::NmrOneD 322764 Specdb::NmrOneD 322765 Specdb::NmrOneD 322766 Specdb::NmrOneD 322767 Specdb::NmrOneD 322768 Specdb::NmrOneD 322769 Specdb::NmrOneD 322770 Specdb::NmrOneD 322771 Specdb::MsMs 28379 Specdb::MsMs 28380 Specdb::MsMs 28381 Specdb::MsMs 34937 Specdb::MsMs 34938 Specdb::MsMs 34939 742 114525 C03741 15757 GLUTAMATE-1-SEMIALDEHYDE GLU_LSN3_DHE2 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 Glutamyl-tRNA reductase P0A6X1 HEM1_ECOLI hemA http://ecmdb.ca/proteins/P0A6X1.xml Glutamate-1-semialdehyde 2,1-aminomutase P23893 GSA_ECOLI hemL http://ecmdb.ca/proteins/P23893.xml (S)-4-Amino-5-oxopentanoate <> 5-Aminolevulinic acid R02272 GSAAMINOTRANS-RXN L-Glutamyl-tRNA(Glu) + Hydrogen ion + NADPH > (S)-4-Amino-5-oxopentanoate + NADP + tRNA (Glu) 5-Aminolevulinic acid <> (S)-4-Amino-5-oxopentanoate R02272 GSAAMINOTRANS-RXN L-Glutamyl-tRNA(Glu) + NADPH + Hydrogen ion + tRNA(Glu) <> (S)-4-Amino-5-oxopentanoate + tRNA(Glu) + NADP + L-Glutamyl-tRNA(Glu) R04109 (S)-4-Amino-5-oxopentanoate > 5-Aminolevulinic acid (S)-4-Amino-5-oxopentanoate + NADP + tRNA(Glu) > L-glutamyl-tRNA(Glu) + NADPH 8 L-glutamyl-tRNA(Glu) + 8 NADPH + 8 NADPH >8 tRNA(Glu) +8 NADP +8 (S)-4-Amino-5-oxopentanoate PW_R003473 8 (S)-4-Amino-5-oxopentanoate >8 5-Aminolevulinic acid PW_R003474 (S)-4-Amino-5-oxopentanoate <>5 5-Aminolevulinic acid 5 5-Aminolevulinic acid <> (S)-4-Amino-5-oxopentanoate L-Glutamyl-tRNA(Glu) + NADPH + Hydrogen ion + tRNA(Glu) <> (S)-4-Amino-5-oxopentanoate + NADP (S)-4-Amino-5-oxopentanoate <>5 5-Aminolevulinic acid