Comparative structural studies of the active site of ATP: guanidine phosphotransferases. The essential cysteine tryptic peptide of taurocyamine kinase from Arenicola marina.
The active cysteinyl residues of dimeric taurocyamine kinase from Arenicola marina were labelled with N-ethyl-[1-14C]maleimide. The resulting inactivated N-ethyl-[1-14C]succinimido enzyme was then subjected to tryptic hydrolysis. The peptide containing the labelled essential cysteinyl residue was isolated. The amino acid sequence of this peptide is Leu-Gly-Tyr-Leu-Gly-Thr-[14C]-Cys-Pro-Thr-Asn-Ile-Gly-Leu-Arg. This sequence is very similar to that of homologous ATP:guanidine phosphotransferases previously studied, arginine kinase from Homarus vulgaris muscle, creatine kinase from ox brain and ox muscle, and from rabbit muscle, and lombricine kinase from Lubricus terrestris.
D000476:Alkanesulfonates; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D003545:Cysteine / Q000032:analysis; D005033:Ethylmaleimide; D006146:Guanidines; D010446:Peptide Fragments / Q000032:analysis; D010770:Phosphotransferases; D011077:Polychaeta / Q000201:enzymology*; D011485:Protein Binding; D013381:Subtilisins; D013388:Succinimides; D013656:Taurocholic Acid; D013820:Thermolysin; D014357:Trypsin
D000476:Alkanesulfonates; D000596:Amino Acids; D006146:Guanidines; D010446:Peptide Fragments; D013388:Succinimides; D013656:Taurocholic Acid; D010770:Phosphotransferases; D013381:Subtilisins; D014357:Trypsin; D013820:Thermolysin; D003545:Cysteine; D005033:Ethylmaleimide