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  Phosphoenol pyruvate‐dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system

Dörschug, M., Frank, R., Kalbitzer, H. R., Hengstenberg, W., & Deutscher, J. (1984). Phosphoenol pyruvate‐dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system. European Journal of Biochemistry, 144(1), 113-119. doi:10.1111/j.1432-1033.1984.tb08438.x.

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EurJBiochem_144_1984_113.pdf (beliebiger Volltext), 615KB
 
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 Urheber:
Dörschug, Michael, Autor
Frank, Rainer1, Autor           
Kalbitzer, Hans Robert2, Autor           
Hengstenberg, Wolfgang1, Autor           
Deutscher, Josef1, Autor           
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Zusammenfassung: Enzyme‐IIIglc is part of the glucose phosphotransferase system of Escherichia coli and Salmonella typhimurium and is phosphorylated by phosphorenol pyruvate in a reaction requiring enzyme I (phosphorenol pyruvate‐protein phosphotransferase), and the histidine‐containing phospho‐carrier protein HPr. In this paper we report the isolation of IIIglc from E. coli and the characterization of the active center. Alkaline hydrolysis of [32P]P ‐IIIglc and chromatography of the hydrolysate suggested that the phosphoryl group is bound to a histidyl residue in P ‐IIIglc of S. typhimurium. Here we present 1H‐NMR measurements of IIIglc and P ‐IIIglc from E. coli which further substantiate that the phosphoryl group in P ‐IIIglc is linked to the N‐3 position of a histidyl residue. After phosporylation of IIIglc with [32P]Phosphoenol pyruvate, enzyme I and HPr, the phosphorylated protein was cleaved with either alkaline protease from Streptomyces griseus or subtilisin from Bacillus subtilis. According to amino acid analysis both proteases produced the same peptide carrying the phosphoryl group. The amino acid sequence of this peptide was found to be Val‐His‐Phe‐Gly‐Ile‐Asp. The lower electrophoretic mobility of P ‐IIIglc on dodecylsulfate/polyacrylamide gels and its stronger binding to the hydrophobic matrix of a reversed‐phase column compared to unphosphorylated protein may indicate a structural change following phosphoenolpyruvate‐dependent phosphorylation.

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Sprache(n): eng - English
 Datum: 1984-04-161984-06-251984-10
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1111/j.1432-1033.1984.tb08438.x
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Titel: European Journal of Biochemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Seiten: - Band / Heft: 144 (1) Artikelnummer: - Start- / Endseite: 113 - 119 Identifikator: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040