2.0 2012-05-31 14:53:09 -0600 2015-06-03 17:20:22 -0600 ECMDB20608 M2MDB001407 L-Seryl-AMP L-Seryl-AMP is an enzyme-bound intermediate found in the protein EntF. EntF is the enzyme responsible for serine activation during the biosynthesis of enterobactin (a cyclic trimer of N-dihydroxybenzoyl serine) in Escherichia coli. Serine adenylate is also an intermediate in the charging of Seryl-tRNA-synthetase. In particular, Mg.ATP and serine react to form seryl-adenylate on the protein. The serine is subsequently transferred to the 3'-end of the tRNA. Seryl-tRNA synthetase is also capable of synthesizing diadenosine tetraphosphate (Ap4A) from the enzyme-bound seryl-adenylate intermediate and a second molecule of ATP. (L-Seryl)adenylate (L-Seryl)adenylic acid L-Serine adenylate L-Serine adenylic acid L-Serine AMP L-Seryl-adenylate L-Seryl-adenylic acid Serine adenylate Serine adenylic acid Serine AMP Seryl adenylate Seryl adenylic acid Seryl-AMP SRP C13H19N6O9P 434.2985 434.095112748 {[(2S)-2-amino-3-hydroxypropanoyl]oxy}({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid L-seryl-AMP 52435-67-3 [H][C@](N)(CO)C(=O)OP(O)(=O)OC[C@@]1([H])O[C@@]([H])(N2C=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O InChI=1S/C13H19N6O9P/c14-5(1-20)13(23)28-29(24,25)26-2-6-8(21)9(22)12(27-6)19-4-18-7-10(15)16-3-17-11(7)19/h3-6,8-9,12,20-22H,1-2,14H2,(H,24,25)(H2,15,16,17)/t5-,6+,8+,9+,12+/m0/s1 UVSYURUCZPPUQD-MACXSXHHSA-N Cytosol logp -2.34 ALOGPS logs -2.15 ALOGPS solubility 3.07e+00 g/l ALOGPS logp -4.6 ChemAxon pka_strongest_acidic 0.77 ChemAxon pka_strongest_basic 6.83 ChemAxon iupac {[(2S)-2-amino-3-hydroxypropanoyl]oxy}({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid ChemAxon average_mass 434.2985 ChemAxon mono_mass 434.095112748 ChemAxon smiles [H][C@](N)(CO)C(=O)OP(O)(=O)OC[C@@]1([H])O[C@@]([H])(N2C=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O ChemAxon formula C13H19N6O9P ChemAxon inchi InChI=1S/C13H19N6O9P/c14-5(1-20)13(23)28-29(24,25)26-2-6-8(21)9(22)12(27-6)19-4-18-7-10(15)16-3-17-11(7)19/h3-6,8-9,12,20-22H,1-2,14H2,(H,24,25)(H2,15,16,17)/t5-,6+,8+,9+,12+/m0/s1 ChemAxon inchikey UVSYURUCZPPUQD-MACXSXHHSA-N ChemAxon polar_surface_area 238.39 ChemAxon refractivity 92.62 ChemAxon polarizability 38.14 ChemAxon rotatable_bond_count 8 ChemAxon acceptor_count 12 ChemAxon donor_count 6 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Specdb::CMs 1083862 Specdb::EiMs 3680 Specdb::NmrOneD 282809 Specdb::NmrOneD 282810 Specdb::NmrOneD 282811 Specdb::NmrOneD 282812 Specdb::NmrOneD 282813 Specdb::NmrOneD 282814 Specdb::NmrOneD 282815 Specdb::NmrOneD 282816 Specdb::NmrOneD 282817 Specdb::NmrOneD 282818 Specdb::NmrOneD 282819 Specdb::NmrOneD 282820 Specdb::NmrOneD 282821 Specdb::NmrOneD 282822 Specdb::NmrOneD 282823 Specdb::NmrOneD 282824 Specdb::NmrOneD 282825 Specdb::NmrOneD 282826 Specdb::NmrOneD 282827 Specdb::NmrOneD 282828 Specdb::MsMs 25868 Specdb::MsMs 25869 Specdb::MsMs 25870 Specdb::MsMs 32426 Specdb::MsMs 32427 Specdb::MsMs 32428 5289403 4451381 SERYL-AMP SRP 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 van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. 17765195 Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. 18331064 Enterobactin synthase component F P11454 ENTF_ECOLI entF http://ecmdb.ca/proteins/P11454.xml 4'-phosphopantetheinyl transferase entD P19925 ENTD_ECOLI entD http://ecmdb.ca/proteins/P19925.xml 3 (2,3-Dihydroxybenzoyl)adenylic acid + 3 L-Seryl-AMP >6 Adenosine monophosphate + Enterochelin +9 Hydrogen ion ENTG-RXN Adenosine triphosphate + Hydrogen ion + L-Serine <> Pyrophosphate + L-Seryl-AMP ENTF-RXN Adenosine triphosphate + L-Serine <> Pyrophosphate + L-Seryl-AMP ENTF-RXN (2,3-Dihydroxybenzoyl)adenylic acid + L-Seryl-AMP <> Hydrogen ion + Enterochelin + Adenosine monophosphate ENTG-RXN Adenosine triphosphate + L-Serine > Pyrophosphate + L-Seryl-AMP