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Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins.

Kruse, R. and Hengstenberg, W. and Beneicke, W. and Kalbitzer, Hans Robert (1993) Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins. Protein engineering 6 (4), pp. 417-423.

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Abstract

The phosphocarrier HPr (heat stable protein) of Staphylococcus carnosus was modified by site-directed mutagenesis of the corresponding ptsH gene in order to analyse the importance of amino acids which were supposed to be part of the active centre of the protein. Three residues which are conserved in all HPrs, Arg17, Pro18 and Glu84, were mutated: Arg17 was changed to His (17RH) and Pro18 and ...

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Item Type:Article
Date:1993
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
8332599PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Bacterial ProteinsMESH
Base SequenceMESH
Binding SitesMESH
Gene ExpressionMESH
Histidine/analysisMESH
Hydrogen-Ion ConcentrationMESH
KineticsMESH
Magnetic Resonance SpectroscopyMESH
Molecular Sequence DataMESH
Mutagenesis, Site-DirectedMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/metabolismMESH
PhosphorylationMESH
Protein ConformationMESH
Staphylococcus/enzymologyMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:08 Sep 2010 08:36
Last Modified:08 Sep 2010 08:36
Item ID:16488
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