Oligomeric interactions provide alternatives to direct steric modes of control of sugar kinase/actin/hsp70 superfamily functions by heterotropic allosteric effectors: Inhibition of E. coli glycerol kinase

Archives of Biochemistry and Biophysics

Volumn 492, Issue 1-2, 2009, Pages 29-39

  Pettigrew, Donald W ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Allostery; Enzyme kinetics; Forster resonance energy transfer; Linked functions

Indexed keywords

ACTIN; ALANINE; ARGININE; FRUCTOSE 1,6 BISPHOSPHATE; GLYCEROL KINASE; HEAT SHOCK PROTEIN 70; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; THREONINE;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING KINETICS; CATALYSIS; CONTROLLED STUDY; ENZYME INHIBITION; ENZYME KINETICS; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; STEREOCHEMISTRY;

ACTINS; ALANINE; ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; ARGININE; CATALYTIC DOMAIN; DIMERIZATION; DRUG INTERACTIONS; ESCHERICHIA COLI PROTEINS; GLYCEROL KINASE; HSP70 HEAT-SHOCK PROTEINS; MULTIGENE FAMILY; PROTEIN SUBUNITS; STEREOISOMERISM;

ESCHERICHIA COLI;

EID: 70450222702     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.10.001     Document Type: Article

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