Ground State Destabilization by Anionic Nucleophiles Contributes to the Activity of Phosphoryl Transfer Enzymes

PLoS Biology

Volumn 11, Issue 7, 2013, Pages

  Andrews, Logan D ^a   Fenn, Tim D ^b   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

^b Stanford University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALKALINE PHOSPHATASE; CHEMICAL COMPOUND; GLYCINE; NUCLEOPHILE; PROTEIN TYROSINE PHOSPHATASE; SERINE; TUNGSTIC ACID; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GROUND STATE DESTABILIZATION; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; MUTATION RATE; PH MEASUREMENT; STATIC ELECTRICITY; STRUCTURE ANALYSIS; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ALKALINE PHOSPHATASE; CATALYTIC DOMAIN; HYDROGEN-ION CONCENTRATION; MUTATION; PHOSPHATES; SERINE;

EID: 84880965304     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001599     Document Type: Article

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