Seryl transfer ribonucleic acid synthetase from Escherichia coli. Substrate binding and chemical modification of cysteinyl residues.
D000255:Adenosine Triphosphate; D000478:Alkylation; D000577:Amides; D000596:Amino Acids / Q000032:analysis; D000604:Amino Acyl-tRNA Synthetases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D001565:Benzoates; D001665:Binding Sites; D002247:Carbon Isotopes; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D003545:Cysteine; D004220:Disulfides; D004926:Escherichia coli / Q000201:enzymology*; D007461:Iodoacetates; D007525:Isoelectric Focusing; D008626:Mercuribenzoates; D010759:Phosphorus Isotopes; D011485:Protein Binding; D012694:Serine; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000032:analysis; D014508:Urea
D000577:Amides; D000596:Amino Acids; D001565:Benzoates; D002247:Carbon Isotopes; D004220:Disulfides; D007461:Iodoacetates; D008626:Mercuribenzoates; D010759:Phosphorus Isotopes; D013438:Sulfhydryl Compounds; D012694:Serine; D000255:Adenosine Triphosphate; D014508:Urea; D000604:Amino Acyl-tRNA Synthetases; D003545:Cysteine