This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Aminoacyl-tRNA Charging|
Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655
This pathway groups together all Escherichia coli tRNA charging reactions.
Unification Links: EcoCyc:TRNA-CHARGING-PWY
Abibi14: Abibi A, Ferguson AD, Fleming PR, Gao N, Hajec LI, Hu J, Laganas VA, McKinney DC, McLeod SM, Prince DB, Shapiro AB, Buurman ET (2014). "The role of a novel auxiliary pocket in bacterial phenylalanyl-tRNA synthetase druggability." J Biol Chem 289(31);21651-62. PMID: 24936059
Ahel02: Ahel I, Stathopoulos C, Ambrogelly A, Sauerwald A, Toogood H, Hartsch T, Soll D (2002). "Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases." J Biol Chem 277(38);34743-8. PMID: 12130657
Akesson78: Akesson B, Lundvik L (1978). "Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli." Eur J Biochem 83(1);29-36. PMID: 342244
Aldinger12: Aldinger CA, Leisinger AK, Igloi GL (2012). "The influence of identity elements on the aminoacylation of tRNA(Arg) by plant and Escherichia coli arginyl-tRNA synthetases." FEBS J 279(19);3622-38. PMID: 22831759
Andrews85: Andrews D, Trezeguet V, Merle M, Graves PV, Muench KH, Labouesse B (1985). "Tryptophanamide formation by Escherichia coli tryptophanyl-tRNA synthetase." Eur J Biochem 146(1);201-9. PMID: 3881255
Ankilova75: Ankilova VN, Vlassov VV, Knorre DG, Melamed NV, Nuzdihna NA (1975). "Involvement of the D-stem of tRNAPhe (E. coli) in interaction with phenylalanyl-tRNA synthetase as shown by chemical modification." FEBS Lett 60(1);168-71. PMID: 776674
Anselme91: Anselme J, Hartlein M (1991). "Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding." FEBS Lett 280(1);163-6. PMID: 2009959
Aoki92: Aoki H, Yaworsky PJ, Patel SD, Margolin-Brzezinski D, Park KS, Ganoza MC (1992). "The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316." Eur J Biochem 209(2);511-21. PMID: 1425658
Archibold72: Archibold ER, Williams LS (1972). "Regulation of synthesis of methionyl-, prolyl-, and threonyl-transfer ribonucleic acid synthetases of Escherichia coli." J Bacteriol 109(3);1020-6. PMID: 4551738
Archontis01: Archontis G, Simonson T, Karplus M (2001). "Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase." J Mol Biol 306(2);307-27. PMID: 11237602
Archontis01a: Archontis G, Simonson T (2001). "Dielectric relaxation in an enzyme active site: molecular dynamics simulations interpreted with a macroscopic continuum model." J Am Chem Soc 123(44);11047-56. PMID: 11686711
Archontis98: Archontis G, Simonson T, Moras D, Karplus M (1998). "Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations." J Mol Biol 275(5);823-46. PMID: 9480772
Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699
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