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Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus: ¹H nuclear magnetic resonance studies on phosphorylated and unphosphorylated factor IIIlac and its interaction with the phosphocarrier protein HPr

Kalbitzer, Hans Robert and Deutscher, J. and Hengstenberg, W. and Rösch, P. (1981) Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus: ¹H nuclear magnetic resonance studies on phosphorylated and unphosphorylated factor IIIlac and its interaction with the phosphocarrier protein HPr. Biochemistry 20 (21), pp. 6178-6185.

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Abstract

The trimeric phosphocarrier protein factor III specific for galactosides was investigated by 1H NMR spectroscopy. The protomer contains four histidyl residues with acidic pK values in the range 5.6-6.2. One of the histidyl residues, His-B, carries the phosphoryl group. The pK value of His-B increases from 6.0 to 8.6 upon phosphorylation. To determine the position of the phosphoryl group with ...

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Item Type:Article
Date:1981
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
7306504PubMed ID
Classification:
NotationType
Bacterial ProteinsMESH
Carrier Proteins/metabolismMESH
Hydrogen-Ion ConcentrationMESH
KineticsMESH
Magnetic Resonance SpectroscopyMESH
Peptide Fragments/analysisMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/metabolismMESH
Phosphoproteins/metabolismMESH
PhosphorylationMESH
Staphylococcus aureus/enzymologyMESH
TrypsinMESH
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 06:29
Last Modified:02 Sep 2010 06:29
Item ID:16427
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