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Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system

Dörschug, M. and Frank, R. and Kalbitzer, Hans Robert and Hengstenberg, W. and Deutscher, J. (1984) Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system. European journal of biochemistry / FEBS 144 (1), pp. 113-119.

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Abstract

Enzyme-IIIglc is part of the glucose phosphotransferase system of Escherichia coli and Salmonella typhimurium and is phosphorylated by phosphoenolpyruvate in a reaction requiring enzyme I (phosphoenolpyruvate-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 ...

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Item Type:Article
Date:1984
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
6383826PubMed ID
Classification:
NotationType
Binding SitesMESH
Chemical PhenomenaMESH
ChemistryMESH
Electrophoresis, Polyacrylamide GelMESH
Escherichia coli/enzymologyMESH
Escherichia coli ProteinsMESH
Magnetic Resonance SpectroscopyMESH
Peptides/isolation & purificationMESH
Phosphoenolpyruvate/physiologyMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/metabolismMESH
PhosphorylationMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:02 Sep 2010 06:32
Last Modified:02 Sep 2010 06:32
Item ID:16436
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