Allostery is an intrinsic property of the protease domain of DegS: Implications for enzyme function and evolution

Journal of Biological Chemistry

Volumn 285, Issue 44, 2010, Pages 34039-34047

  Sohn, Jungsan ^a   Grant, Robert A ^a   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERY; ENZYME FUNCTIONS; FUNCTIONAL CONFORMATIONS; INITIAL RATE; INTRINSIC FEATURES; INTRINSIC PROPERTY; MAXIMAL VELOCITY; NON-FUNCTIONAL; OUTER MEMBRANE; PDZ DOMAINS; PROTEIN SUBSTRATE; PROTEOLYTIC CASCADE; STRESS RESPONSE GENES; SUBSTRATE BINDING; TERTIARY STRUCTURES; TWO-STATE MODEL;

CONFORMATIONS; CYTOLOGY; ENZYMES; ESCHERICHIA COLI; PROTEIN FOLDING; TRANSCRIPTION;

SUBSTRATES;

HYBRID PROTEIN; PDZ PROTEIN; PROTEIN DEGS; PROTEINASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT; REGULATORY MECHANISM;

ALLOSTERIC SITE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; HYDROGEN BONDING; KINETICS; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

ESCHERICHIA COLI;

EID: 77958563467     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.135541     Document Type: Article

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