Conformational stability changes of the amino terminal domain of enzyme I of the escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: Implications for phosphorylation effects

Protein Science

Volumn 9, Issue 6, 2000, Pages 1085-1094

  Ginsburg, Ann ^a   Szczepanowski, Roman H ^a   Ruvinov, Sergei B ^a,d   Nosworthy, Neil J ^b,e   Sondej, Melissa ^b   Umland, Timothy C ^c   Peterkofsky, Alan ^b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^c NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^d NATIONAL CANCER INSTITUTE   (United States)

^e UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Active site mutants H189E and H189A; Amino terminal domain; Differential scanning calorimetry; Enzyme I of the E. coli phosphoenolpyruvate:sugar phosphotransferase system; Phosphorylation; Secondary structure; Thermal stability

Indexed keywords

ALANINE; BACTERIAL ENZYME; GLUTAMIC ACID; HISTIDINE; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MODIFICATION; ENZYME STABILITY; ESCHERICHIA COLI; GENETIC ENGINEERING; MUTATION; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA;

EID: 0033945086     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.6.1085     Document Type: Article

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