Individual substitutions of clustered arginine residues of the sensor kinase KdpD of Escherichia coli modulate the ratio of kinase to phosphatase activity

Journal of Biological Chemistry

Volumn 273, Issue 41, 1998, Pages 26415-26420

  Jung, Kirsten ^a   Altendorf, Karlheinz ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PHOSPHATASE; PHOSPHOTRANSFERASE;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; BACTERIAL PROTEINS; BLOTTING, WESTERN; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHOTRANSFERASES; PROTEIN KINASES; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032500535     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.41.26415     Document Type: Article

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