Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes

Journal of the American Chemical Society

Volumn 130, Issue 12, 2008, Pages 3952-3958

  Baxter, Nicola J ^a   Blackburn, G Michael ^a   Marston, James P ^a   Hounslow, Andrea M ^a   Cliff, Matthew J ^a   Bermel, Wolfgang ^b   Williams, Nicholas H ^a   Hollfelder, Florian ^c   Wemmer, David E ^d   Waltho, Jonathan P ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b BRUKER BIOSPIN GMBH   (Germany)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COORDINATED FLUORIDES; GEOBACILLUS STEAROTHERMOPHILUS; NUCLEOTIDE KINASES; TRANSITION STATE ANALOGS (TSA);

BACTERIA; ENZYMES; FLUORINE COMPOUNDS; METAL COMPLEXES; REACTION KINETICS;

CHARGE TRANSFER;

ALUMINUM; BETA PHOSPHOGLUCOMUTASE; INORGANIC SALT; MAGNESIUM FLUORIDE; PHOSPHATASE; PHOSPHOGLUCOMUTASE; PHOSPHOGLYCERATE KINASE; PHOSPHOSERINE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTALLIZATION; ELECTRICITY; GEOBACILLUS STEAROTHERMOPHILUS; GEOMETRY; LACTOCOCCUS LACTIS; METHANOCOCCUS JANNASCHII; NUCLEAR MAGNETIC RESONANCE; PH; PROTEIN TRANSPORT;

ALUMINUM COMPOUNDS; ANIONS; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; CATALYSIS; FLUORIDES; HYDROGEN-ION CONCENTRATION; LIGANDS; MAGNESIUM COMPOUNDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PHOSPHOGLYCERATE KINASE; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHOTRANSFERASES (PHOSPHOMUTASES); PROTEIN STRUCTURE, TERTIARY; REFERENCE STANDARDS;

EID: 41149163674     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja078000n     Document Type: Article

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