2.0 2012-05-31 10:27:06 -0600 2015-09-13 12:56:08 -0600 ECMDB00510 M2MDB000144 Aminoadipic acid Aminoadipic acid is metabolite in the principal biochemical pathway of lysine. The major outer membrane proteins from Escherichia coli K-12 are often modified to contain alpha-aminoadipic acid delta-semialdehyde (allysine). [PMID:358196]. Amiinoadipic acid can be decarboxylated by glutmate decarboxylase [PMID:379598] (+/-)-2-Aminoadipate (+/-)-2-Aminoadipic acid 2-Aminoadipate 2-Aminoadipic acid a-amino-Adipate a-amino-Adipic acid A-Aminoadipate A-Aminoadipic acid alpha-amino-Adipate Alpha-Amino-adipic acid Alpha-Aminoadipate Alpha-Aminoadipic acid Aminoadipate DL-2-Aminoadipate DL-2-Aminoadipic acid DL-2-Aminohexanedioate DL-2-Aminohexanedioic acid DL-a-Aminoadipate DL-a-Aminoadipic acid DL-alpha-Aminoadipate DL-alpha-Aminoadipic acid DL-α-Aminoadipate DL-α-Aminoadipic acid L-2-aminoadipate L-2-Aminoadipic acid L-2-Aminohexanedioate L-2-Aminohexanedioic acid L-a-Aminoadipate L-a-Aminoadipic acid L-alpha-Aminoadipate L-alpha-Aminoadipic acid L-α-Aminoadipate L-α-Aminoadipic acid α-amino-Adipate α-amino-Adipic acid α-Aminoadipate α-Aminoadipic acid C6H11NO4 161.1558 161.068807845 (2S)-2-aminohexanedioic acid aminoadipate 542-32-5 N[C@@H](CCCC(O)=O)C(O)=O InChI=1S/C6H11NO4/c7-4(6(10)11)2-1-3-5(8)9/h4H,1-3,7H2,(H,8,9)(H,10,11)/t4-/m0/s1 OYIFNHCXNCRBQI-BYPYZUCNSA-N Solid Cytoplasm Periplasm logp -3.43 ALOGPS logs -0.69 ALOGPS solubility 3.27e+01 g/l ALOGPS melting_point 196-198 oC logp -2.8 ChemAxon pka_strongest_acidic 2.01 ChemAxon pka_strongest_basic 9.53 ChemAxon iupac (2S)-2-aminohexanedioic acid ChemAxon average_mass 161.1558 ChemAxon mono_mass 161.068807845 ChemAxon smiles N[C@@H](CCCC(O)=O)C(O)=O ChemAxon formula C6H11NO4 ChemAxon inchi InChI=1S/C6H11NO4/c7-4(6(10)11)2-1-3-5(8)9/h4H,1-3,7H2,(H,8,9)(H,10,11)/t4-/m0/s1 ChemAxon inchikey OYIFNHCXNCRBQI-BYPYZUCNSA-N ChemAxon polar_surface_area 100.62 ChemAxon refractivity 35.89 ChemAxon polarizability 15.53 ChemAxon rotatable_bond_count 5 ChemAxon acceptor_count 5 ChemAxon donor_count 3 ChemAxon physiological_charge -1 ChemAxon formal_charge 0 ChemAxon 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 Lysine degradation ec00310 Specdb::CMs 1382 Specdb::CMs 2707 Specdb::CMs 133849 Specdb::CMs 141583 Specdb::CMs 1064546 Specdb::CMs 1064548 Specdb::CMs 1064550 Specdb::CMs 1064552 Specdb::CMs 1064554 Specdb::CMs 1064555 Specdb::CMs 1064557 Specdb::CMs 1064559 Specdb::CMs 1064561 Specdb::CMs 1064563 Specdb::CMs 1064564 Specdb::CMs 1064566 Specdb::CMs 1064568 Specdb::CMs 1064570 Specdb::NmrOneD 6982 Specdb::NmrOneD 6983 Specdb::NmrOneD 6984 Specdb::NmrOneD 6985 Specdb::NmrOneD 6986 Specdb::NmrOneD 6987 Specdb::NmrOneD 6988 Specdb::NmrOneD 6989 Specdb::NmrOneD 6990 Specdb::NmrOneD 6991 Specdb::NmrOneD 6992 Specdb::NmrOneD 6993 Specdb::NmrOneD 6994 Specdb::NmrOneD 6995 Specdb::NmrOneD 6996 Specdb::NmrOneD 6997 Specdb::NmrOneD 6998 Specdb::NmrOneD 6999 Specdb::NmrOneD 7000 Specdb::NmrOneD 7001 Specdb::MsMs 27206 Specdb::MsMs 27207 Specdb::MsMs 27208 Specdb::MsMs 33764 Specdb::MsMs 33765 Specdb::MsMs 33766 Specdb::MsMs 2226781 Specdb::MsMs 2227958 Specdb::MsMs 2229186 Specdb::MsMs 2230256 Specdb::MsMs 2231656 Specdb::MsMs 2232558 Specdb::MsMs 2233985 Specdb::MsMs 2234927 Specdb::MsMs 2235952 Specdb::MsMs 2237451 Specdb::MsMs 2238017 Specdb::MsMs 2239539 Specdb::MsMs 2240190 Specdb::MsMs 2241538 Specdb::MsMs 2242270 Specdb::MsMs 2243576 Specdb::MsMs 2246490 Specdb::MsMs 2247800 Specdb::MsMs 2252754 HMDB00510 83182 C00956 17082 UN1 alpha-Aminoadipate 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 Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. 18402659 Sukhareva, B. S., Malikova, D. G. (1977). "[Substrate specificity of E. coli glutamate decarboxylase]." Mol Biol (Mosk) 11:394-402. 379598 Diedrich, D. L., Schnaitman, C. A. (1978). "Lysyl-derived aldehydes in outer membrane proteins of Escherichia coli." Proc Natl Acad Sci U S A 75:3708-3712. 358196 Waalkes, T.P. etal., J.A.C.S., 1950, 72, 5760; Trown, P.W. etal., Biochem. J., 1963, 86, 280-284; Lerch, E. etal., Helv. Chim. Acta, 1974, 57, 1584-1597; Kondo, M. etal., Bull. Chem. Soc. Jpn., 1985, 58, 1171-1173 http://hmdb.ca/system/metabolites/msds/000/000/429/original/HMDB00510.pdf?1358461812 Glutamate decarboxylase alpha P69908 DCEA_ECOLI gadA http://ecmdb.ca/proteins/P69908.xml Glutamate decarboxylase beta P69910 DCEB_ECOLI gadB http://ecmdb.ca/proteins/P69910.xml