Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization

Journal of the American Chemical Society

Volumn 133, Issue 30, 2011, Pages 11621-11631

  Andrews, Logan D ^a   Deng, Hua ^b   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALKALINE PHOSPHATASE; BINDING AFFINITIES; DIANIONS; ELECTROSTATIC REPULSION; FOURIER TRANSFORM INFRARED; FTIR; INORGANIC PHOSPHATES; IONIC STRUCTURE; LIGAND BINDING PROPERTIES; NEGATIVE CHARGE; OXYANIONS; PH-DEPENDENT; PHOSPHATE ESTERS; PHOSPHATE MONOESTERS; PHOSPHORYL GROUPS; PRODUCT INHIBITION; RELATED COMPOUNDS; STRONG INTERACTION; SUBSTRATE SATURATION; TRANSITION STATE;

ALKALINITY; AMINO ACIDS; BINDING ENERGY; CATALYSIS; ELECTROSTATICS; ESCHERICHIA COLI; FOURIER TRANSFORMS; GROUND STATE; ISOTOPES; LIGANDS; PROTONS; SUBSTRATES;

PHOSPHATASES;

ALKALINE PHOSPHATASE; PHOSPHATE;

ARTICLE; BINDING AFFINITY; ENERGY TRANSFER; ENZYME INHIBITION; ENZYME SUBSTRATE; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; LIGAND BINDING; NONHUMAN; PH; PHASE TRANSITION; PROTEIN INTERACTION; PROTON TRANSPORT; STATIC ELECTRICITY;

ALKALINE PHOSPHATASE; BINDING SITES; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LIGANDS; OXYGEN ISOTOPES; PHOSPHATES; SERINE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 79960858431     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja203370b     Document Type: Article

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