Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase

Biochemistry

Volumn 45, Issue 17, 2006, Pages 5421-5429

  Williams, Rachel ^a   Holyoak, Todd ^a   McDonald, Gissel ^a   Gui, Chunshan ^a   Fenton, Aron W ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; ALDEHYDES; AMINO ACIDS; BRAIN; HYDROPHOBICITY; MOLECULAR STRUCTURE; MUSCLE; NITROGEN COMPOUNDS;

ALLOSTERIC RESPONSE; ALLOSTERY; BINDING SITE; PYRUVATE KINASE;

ENZYMES;

2 AMINOPROPANALDEHYDE; ALANINE; ALDEHYDE; ISOENZYME; LIGAND; METHYL GROUP; PHENYLALANINE; PHENYLALANINE DERIVATIVE; PROPANE; PYRUVATE KINASE; PYRUVATE KINASE BRAIN ISOENZYME; PYRUVATE KINASE MUSCLE ISOENZYME; UNCLASSIFIED DRUG;

ALLOSTERIC INHIBITION; ALLOSTERISM; AROMATICITY; ARTICLE; BINDING COMPETITION; BINDING SITE; CONFORMATION; ENZYME BINDING; ENZYME INHIBITION; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; REACTION ANALYSIS; STRUCTURE ANALYSIS;

ALANINE; ALLOSTERIC REGULATION; ANIMALS; BINDING, COMPETITIVE; CRYSTALLIZATION; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MUSCLES; PHENYLALANINE; PROTEIN CONFORMATION; PYRUVATE KINASE; RABBITS;

MAMMALIA;

EID: 33646347609     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0524262     Document Type: Article

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