2.0 2012-05-31 13:58:41 -0600 2015-06-03 15:54:22 -0600 ECMDB03357 M2MDB000493 N-Acetylornithine N-Acetylornithine is a intermediate in arginine and proline metabolism pathway. It is converted to ornithine via acetylornithine deacetylase (EC:3.5.1.16). (KEGG) (2S)-2-acetamido-5-aminopentanoate (2S)-2-acetamido-5-aminopentanoic acid N-α-acetylornithine N-acetylornithine N2-acetyl-L-ornithine N2-acetyl-ornithine Acetyl-Ornithine Acetylornithine AOR N(2)-Acetyl-L-ornithine n-α-acetylornithine N-a-Acetylornithine N-AcOrn N-alpha-Acetylornithine N-α-Acetylornithine N2-Acetyl-L-ornithine N2-acetyl-ornithine C7H14N2O3 174.1977 174.100442324 (2S)-5-amino-2-acetamidopentanoic acid N(2)-acetyl-L-ornithine CC(=O)N[C@@H](CCCN)C(O)=O InChI=1S/C7H14N2O3/c1-5(10)9-6(7(11)12)3-2-4-8/h6H,2-4,8H2,1H3,(H,9,10)(H,11,12)/t6-/m0/s1 JRLGPAXAGHMNOL-LURJTMIESA-N Solid Cytosol logp -2.73 ALOGPS logs -0.66 ALOGPS solubility 3.78e+01 g/l ALOGPS logp -3.6 ChemAxon pka_strongest_acidic 3.82 ChemAxon pka_strongest_basic 9.9 ChemAxon iupac (2S)-5-amino-2-acetamidopentanoic acid ChemAxon average_mass 174.1977 ChemAxon mono_mass 174.100442324 ChemAxon smiles CC(=O)N[C@@H](CCCN)C(O)=O ChemAxon formula C7H14N2O3 ChemAxon inchi InChI=1S/C7H14N2O3/c1-5(10)9-6(7(11)12)3-2-4-8/h6H,2-4,8H2,1H3,(H,9,10)(H,11,12)/t6-/m0/s1 ChemAxon inchikey JRLGPAXAGHMNOL-LURJTMIESA-N ChemAxon polar_surface_area 92.42 ChemAxon refractivity 42.65 ChemAxon polarizability 17.94 ChemAxon rotatable_bond_count 5 ChemAxon acceptor_count 4 ChemAxon donor_count 3 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Arginine and proline metabolism ec00330 Lysine biosynthesis Lysine is biosynthesized from L-aspartic acid. L-aspartic acid can be incorporated into the cell through various methods: C4 dicarboxylate / orotate:H+ symporter , glutamate / aspartate : H+ symporter GltP, dicarboxylate transporter , C4 dicarboxylate / C4 monocarboxylate transporter DauA, glutamate / aspartate ABC transporter L-aspartic acid is phosphorylated by an ATP-driven Aspartate kinase resulting in ADP and L-aspartyl-4-phosphate. L-aspartyl-4-phosphate is then dehydrogenated through an NADPH driven aspartate semialdehyde dehydrogenase resulting in a release of phosphate, NADP and L-aspartic 4-semialdehyde (involved in methionine biosynthesis). L-aspartic 4-semialdehyde interacts with a pyruvic acid through a 4-hydroxy-tetrahydrodipicolinate synthase resulting in a release of hydrogen ion, water and (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate. The latter compound is then reduced by an NADPH driven 4-hydroxy-tetrahydrodipicolinate reductase resulting in a release of water, NADP and (S)-2,3,4,5-tetrahydrodipicolinate, This compound interacts with succinyl-CoA and water through a tetrahydrodipicolinate succinylase resulting in a release of coenzyme A and N-Succinyl-2-amino-6-ketopimelate. This compound interacts with L-glutamic acid through a N-succinyldiaminopimelate aminotransferase resulting in oxoglutaric acid, N-succinyl-L,L-2,6-diaminopimelate. The latter compound is then desuccinylated by reacting with water through a N-succinyl-L-diaminopimelate desuccinylase resulting in a succinic acid and L,L-diaminopimelate. This compound is then isomerized through a diaminopimelate epimerase resulting in a meso-diaminopimelate (involved in peptidoglyccan biosynthesis I). This compound is then decarboxylated by a diaminopimelate decarboxylase resulting in a release of carbon dioxide and L-lysine. L-lysine is then incorporated into lysine degradation pathway. Lysine also regulate its own biosynthesis by repressing dihydrodipicolinate synthase and also repressing lysine-sensitive aspartokinase 3. A metabolic connection joins synthesis of an amino acid, lysine, to synthesis of cell wall material. Diaminopimelate is a precursor both for lysine and for cell wall components. The synthesis of lysine, methionine and threonine share two reactions at the start of the three pathways, the reactions converting L-aspartate to L-aspartate semialdehyde. The reaction involving aspartate kinase is carried out by three isozymes, one specific for synthesis of each end product amino acid. Each of the three aspartate kinase isozymes is regulated by its corresponding end product amino acid. PW000771 ec00300 Metabolic Metabolic pathways eco01100 arginine metabolism The metabolism of L-arginine starts with the acetylation of L-glutamic acid resulting in a N-acetylglutamic acid while releasing a coenzyme A and a hydrogen ion. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NDPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. L-glutamine is used to synthesize carbamoyl phosphate through the interaction of L-glutamine, water, ATP, and hydrogen carbonate. This reaction yields ADP, L-glutamic acid, phosphate, and hydrogen ion. Carbamoyl phosphate and ornithine are used to catalyze the production of citrulline through an ornithine carbamoyltransferase. Citrulline reacts with L-aspartic acid through an ATP dependent enzyme, argininosuccinate synthase to produce pyrophosphate, AMP and argininosuccinic acid. Argininosussinic acid is then lyase to produce L-arginine and fumaric acid. L-arginine can be metabolized into succinic acid by two different sets of reactions: 1. Arginine reacts with succinyl-CoA through a arginine N-succinyltransferase resulting in N2-succinyl-L-arginine while releasing CoA and Hydrogen Ion. N2-succinyl-L-arginine is then dihydrolase to produce a N2-succinyl-L-ornithine through a N-succinylarginine dihydrolase. This compound in turn reacts with oxoglutaric acid through succinylornithine transaminase resulting in L-glutamic acid and N2-succinyl-L-glutamic acid 5-semialdehyde. This compoud in turn reacts with a NAD dependent dehydrogenase resulting in N2-succinylglutamate while releasing NADH and hydrogen ion. N2-succinylglutamate reacts with water through a succinylglutamate desuccinylase resulting in L-glutamic acid and a succinic acid. The succinic acid is then incorporated in the TCA cycle 2.Argine reacts with carbon dioxide and a hydrogen ion through a biodegradative arginine decarboxylase, resulting in Agmatine. This compound is then transformed into putrescine by reacting with water and an agmatinase, and releasing urea. Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid. Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. L-arginine is eventua lly metabolized into succinic acid which then goes to the TCA cycle PW000790 Metabolic ornithine metabolism In the ornithine biosynthesis pathway of E. coli, L-glutamate is acetylated to N-acetylglutamate by the enzyme N-acetylglutamate synthase, encoded by the argA gene. The acetyl donor for this reaction is acetyl-CoA. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NADPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. Ornithine interacts with hydrogen ion through a Ornithine decarboxylase resulting in a carbon dioxide release and a putrescine Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid. Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. PW000791 Metabolic ornithine biosynthesis GLUTORN-PWY Specdb::CMs 1611 Specdb::CMs 1721 Specdb::CMs 2560 Specdb::CMs 30113 Specdb::CMs 30114 Specdb::CMs 30652 Specdb::CMs 30653 Specdb::CMs 31456 Specdb::CMs 31457 Specdb::CMs 38583 Specdb::CMs 134858 Specdb::CMs 142592 Specdb::NmrOneD 4732 Specdb::NmrOneD 4733 Specdb::NmrOneD 135770 Specdb::NmrOneD 135771 Specdb::NmrOneD 135772 Specdb::NmrOneD 135773 Specdb::NmrOneD 135774 Specdb::NmrOneD 135775 Specdb::NmrOneD 135776 Specdb::NmrOneD 135777 Specdb::NmrOneD 135778 Specdb::NmrOneD 135779 Specdb::NmrOneD 135780 Specdb::NmrOneD 135781 Specdb::NmrOneD 135782 Specdb::NmrOneD 135783 Specdb::NmrOneD 135784 Specdb::NmrOneD 135785 Specdb::NmrOneD 135786 Specdb::NmrOneD 135787 Specdb::NmrOneD 135788 Specdb::NmrOneD 135789 Specdb::MsMs 28142 Specdb::MsMs 28143 Specdb::MsMs 28144 Specdb::MsMs 34700 Specdb::MsMs 34701 Specdb::MsMs 34702 Specdb::MsMs 437127 Specdb::MsMs 437128 Specdb::MsMs 437129 Specdb::MsMs 437130 Specdb::MsMs 437131 Specdb::MsMs 439178 Specdb::MsMs 445556 Specdb::MsMs 445557 Specdb::MsMs 445558 Specdb::MsMs 445559 Specdb::MsMs 445560 Specdb::MsMs 447330 Specdb::MsMs 448126 Specdb::MsMs 448127 Specdb::MsMs 2235701 Specdb::MsMs 2237654 Specdb::MsMs 2237865 Specdb::MsMs 2239721 Specdb::MsMs 2239860 HMDB03357 439232 388369 C00437 16543 N-ALPHA-ACETYLORNITHINE AOR Keseler, I. 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Biochim Biophys Acta. 1979 Nov 1;587(4):638-42. 508804 Acetylornithine/succinyldiaminopimelate aminotransferase P18335 ARGD_ECOLI argD http://ecmdb.ca/proteins/P18335.xml Acetylornithine deacetylase P23908 ARGE_ECOLI argE http://ecmdb.ca/proteins/P23908.xml Succinylornithine transaminase P77581 ASTC_ECOLI astC http://ecmdb.ca/proteins/P77581.xml N-Acetylornithine + alpha-Ketoglutarate <> N-Acetyl-L-glutamate 5-semialdehyde + L-Glutamate R02283 N-Acetylornithine + Water <> Acetic acid + Ornithine + L-Ornithine R00669 ACETYLORNDEACET-RXN N-Acetylornithine + Water <> Acetic acid + Ornithine R00669 N-Acetylornithine + Water > Ornithine + Acetic acid ACETYLORNDEACET-RXN N-Acetylornithine + Oxoglutaric acid < N-Acetyl-L-glutamate 5-semialdehyde + L-Glutamate ACETYLORNTRANSAM-RXN N-Acetylornithine + Oxoglutaric acid > N-Acetyl-L-glutamate 5-semialdehyde + L-Glutamate N-acetyl-L-glutamate + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + N-Acetylornithine PW_R002673 N-Acetylornithine + Water > Acetic acid + L-Ornithine monochlorohydrate/ornithine PW_R002674 N-Acetylornithine + Water > Ornithine + Acetic acid + Ornithine PW_R002694 N-Acetyl-L-glutamate 5-semialdehyde + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + N-Acetylornithine PW_R002675 N-Acetylornithine + alpha-Ketoglutarate <> N-Acetyl-L-glutamate 5-semialdehyde + L-Glutamate N-Acetylornithine + Water <> Acetic acid + Ornithine + L-Ornithine N-Acetylornithine + Water <> Acetic acid + Ornithine + L-Ornithine Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucose Shake flask and filter culture 43.3 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 173200 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerol Shake flask and filter culture 398.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 1592000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetate Shake flask and filter culture 152.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 608000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 14.1 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 56400 0 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776 Luria-Bertani (LB) media Shake flask 0.61 uM true 0.03 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 2427 108 Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602. 17535911