Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5199-5209

  Schlee, Sandra ^a   Deuss, Miriam ^a,b   Bruning, Marc ^c   Ivens, Andreas ^b   Schwab, Thomas ^a   Hellmann, Nadja ^d   Mayans, Olga ^e   Sterner, Reinhard ^a,b  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b UNIVERSITY OF COLOGNE   (Germany)

^c UNIVERSITY OF BASEL   (Switzerland)

^d JOHANNES GUTENBERG UNIVERSITY   (Germany)

^e UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMBIENT TEMPERATURES; ANTHRANILATE; BINDING MODES; COMPLEMENTATION; CONCENTRATION OF; CONFORMATIONAL FLEXIBILITY; DOUBLE MUTANTS; ENZYMATIC ACTIVITIES; HIGH CONCENTRATION; HYPERTHERMOPHILIC ARCHAEON; PHOSPHORIBOSYLTRANSFERASE; PRODUCT RELEASE; SINGLE MUTANT; SULFOLOBUS SOLFATARICUS; THERMAL STABILITY; TURNOVER NUMBER; WILD TYPES; WILD-TYPE ENZYMES;

AMINO ACIDS; BINDING ENERGY; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; ESCHERICHIA COLI; MAGNESIUM; THERMODYNAMIC STABILITY;

ENZYMES;

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; ANTHRANILIC ACID; MAGNESIUM DERIVATIVE; MAGNESIUM ION; PYROPHOSPHORIC ACID DERIVATIVE; TRYPTOPHAN;

AMINO ACID SYNTHESIS; ARTICLE; BACTERIUM MUTANT; BIOSYNTHESIS; CATALYSIS; CHEMICAL REACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CRYSTAL STRUCTURE; ENVIRONMENTAL TEMPERATURE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE LIBRARY; HALF LIFE TIME; MICHAELIS CONSTANT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; STEADY STATE; SULFOLOBUS SOLFATARICUS; THERMOSTABILITY; WILD TYPE;

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; KINETICS; MAGNESIUM; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SULFOLOBUS SOLFATARICUS;

ARCHAEA; ESCHERICHIA COLI; SULFOLOBUS SOLFATARICUS;

EID: 67049100569     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802335s     Document Type: Article

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