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Phosphoenolpyruvate-dependent phosphotransferase system. ¹H NMR studies on chemically modified HPr proteins

Kalbitzer, Hans Robert ; Muss, H. P. ; Engelmann, R. ; Kiltz, H. H. ; Stüber, K. ; Hengstenberg, W.



Abstract

The low-pK tyrosyl residue present in the heat-stable proteins (HPr) of all Gram-positive bacteria studied until now has been labeled by tetranitromethane in the HPr of Bacillus subtilis and Streptococcus faecalis. The nitrotyrosyl derivatives obtained are fully active in the complementation assay. The labeled tyrosyl residues could be identified as Tyr-37 in both proteins. Reinvestigation of the ...

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