Structural characterizations of glycerol kinase: Unraveling phosphorylation-induced long-range activation

Biochemistry

Volumn 48, Issue 2, 2009, Pages 346-356

  Yeh, Joanne I ^a   Kettering, Regina ^a   Saxl, Ruth ^a   Bourand, Alexa ^b   Darbon, Emmanuelle ^b   Joly, Nathalie ^c   Briozzo, Pierre ^b,c   Deutscher, Josef ^b  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b CNRS   (France)

^c AGROPARISTECH   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION LOOPS; ACTIVE SITES; CONFORMATIONAL CHANGES; CONFORMATIONAL STABILITIES; DIMER INTERFACES; ENTEROCOCCUS CASSELIFLAVUS; ENZYMATIC ACTIVITIES; FAVORABLE INTERACTIONS; GLYCEROL KINASE; HISTIDINE RESIDUES; MUTANT ENZYMES; PAIR-WISE INTERACTIONS; PHOSPHATE PRODUCTIONS; PHOSPHORYL TRANSFERS; STRUCTURAL CHANGES; STRUCTURAL CHARACTERIZATIONS; THERMAL FACTORS; WILD TYPES;

CATALYSTS; CHEMICAL REACTIONS; CONFORMATIONS; ENZYME ACTIVITY; ENZYMES; FATTY ACIDS; HYDROGEN; HYDROGEN BONDS; HYDROGEN PRODUCTION; METABOLISM; PHOSPHORYLATION; SIGNAL TRANSDUCTION; SUGAR (SUCROSE); SUGARS;

GLYCEROL;

ADENOSINE TRIPHOSPHATE; ARGININE; DIMER; GLUTAMIC ACID; GLYCEROL; GLYCEROL KINASE; GLYCEROPHOSPHATE; HISTIDINE; MUTANT PROTEIN; PHOSPHATE; PROTEIN SUBUNIT;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENTEROCOCCUS CASSELIFLAVUS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; WILD TYPE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITE; CATALYSIS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENTEROCOCCUS; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ENTEROCOCCUS CASSELIFLAVUS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENTEROCOCCUS; ENZYME ACTIVATION; GLYCEROL; GLYCEROL KINASE; HISTIDINE; HYDROGEN BONDING; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY;

EID: 59849123384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8009407     Document Type: Article

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