2.02012-05-31 10:27:06 -06002015-09-13 12:56:08 -0600ECMDB00510M2MDB000144Aminoadipic acidAminoadipic 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 acid2-Aminoadipate2-Aminoadipic acida-amino-Adipatea-amino-Adipic acidA-AminoadipateA-Aminoadipic acidalpha-amino-AdipateAlpha-Amino-adipic acidAlpha-AminoadipateAlpha-Aminoadipic acidAminoadipateDL-2-AminoadipateDL-2-Aminoadipic acidDL-2-AminohexanedioateDL-2-Aminohexanedioic acidDL-a-AminoadipateDL-a-Aminoadipic acidDL-alpha-AminoadipateDL-alpha-Aminoadipic acidDL-α-AminoadipateDL-α-Aminoadipic acidL-2-aminoadipateL-2-Aminoadipic acidL-2-AminohexanedioateL-2-Aminohexanedioic acidL-a-AminoadipateL-a-Aminoadipic acidL-alpha-AminoadipateL-alpha-Aminoadipic acidL-α-AminoadipateL-α-Aminoadipic acidα-amino-Adipateα-amino-Adipic acidα-Aminoadipateα-Aminoadipic acidC6H11NO4161.1558161.068807845(2S)-2-aminohexanedioic acidaminoadipate542-32-5N[C@@H](CCCC(O)=O)C(O)=OInChI=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/s1OYIFNHCXNCRBQI-BYPYZUCNSA-NSolidCytoplasmPeriplasmlogp-3.43logs-0.69solubility3.27e+01 g/lmelting_point196-198 oClogp-2.8pka_strongest_acidic2.01pka_strongest_basic9.53iupac(2S)-2-aminohexanedioic acidaverage_mass161.1558mono_mass161.068807845smilesN[C@@H](CCCC(O)=O)C(O)=OformulaC6H11NO4inchiInChI=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/s1inchikeyOYIFNHCXNCRBQI-BYPYZUCNSA-Npolar_surface_area100.62refractivity35.89polarizability15.53rotatable_bond_count5acceptor_count5donor_count3physiological_charge-1formal_charge0Lysine biosynthesisLysine 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.PW000771ec00300MetabolicLysine degradationec00310Specdb::CMs1382Specdb::CMs2707Specdb::CMs133849Specdb::CMs141583Specdb::CMs1064546Specdb::CMs1064548Specdb::CMs1064550Specdb::CMs1064552Specdb::CMs1064554Specdb::CMs1064555Specdb::CMs1064557Specdb::CMs1064559Specdb::CMs1064561Specdb::CMs1064563Specdb::CMs1064564Specdb::CMs1064566Specdb::CMs1064568Specdb::CMs1064570Specdb::NmrOneD6982Specdb::NmrOneD6983Specdb::NmrOneD6984Specdb::NmrOneD6985Specdb::NmrOneD6986Specdb::NmrOneD6987Specdb::NmrOneD6988Specdb::NmrOneD6989Specdb::NmrOneD6990Specdb::NmrOneD6991Specdb::NmrOneD6992Specdb::NmrOneD6993Specdb::NmrOneD6994Specdb::NmrOneD6995Specdb::NmrOneD6996Specdb::NmrOneD6997Specdb::NmrOneD6998Specdb::NmrOneD6999Specdb::NmrOneD7000Specdb::NmrOneD7001Specdb::MsMs27206Specdb::MsMs27207Specdb::MsMs27208Specdb::MsMs33764Specdb::MsMs33765Specdb::MsMs33766Specdb::MsMs2226781Specdb::MsMs2227958Specdb::MsMs2229186Specdb::MsMs2230256Specdb::MsMs2231656Specdb::MsMs2232558Specdb::MsMs2233985Specdb::MsMs2234927Specdb::MsMs2235952Specdb::MsMs2237451Specdb::MsMs2238017Specdb::MsMs2239539Specdb::MsMs2240190Specdb::MsMs2241538Specdb::MsMs2242270Specdb::MsMs2243576Specdb::MsMs2246490Specdb::MsMs2247800Specdb::MsMs2252754HMDB0051083182C0095617082UN1alpha-AminoadipateKanehisa, 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-D114.22080510Vijayendran, 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:R72.18402659Sukhareva, B. S., Malikova, D. G. (1977). "[Substrate specificity of E. coli glutamate decarboxylase]." Mol Biol (Mosk) 11:394-402.379598Diedrich, D. L., Schnaitman, C. A. (1978). "Lysyl-derived aldehydes in outer membrane proteins of Escherichia coli." Proc Natl Acad Sci U S A 75:3708-3712.358196Waalkes, 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, 1171-1173http://hmdb.ca/system/metabolites/msds/000/000/429/original/HMDB00510.pdf?1358461812Glutamate decarboxylase alphaP69908DCEA_ECOLIgadAhttp://ecmdb.ca/proteins/P69908.xmlGlutamate decarboxylase betaP69910DCEB_ECOLIgadBhttp://ecmdb.ca/proteins/P69910.xml