Conformational changes in the activation loop of mitochondrial glutaminase C: A direct fluorescence readout that distinguishes the binding of allosteric inhibitors from activators

Journal of Biological Chemistry

Volumn 292, Issue 15, 2017, Pages 6095-6107

  Stalnecker, Clint A ^a   Erickson, Jon W ^a   Cerione, Richard A ^a,b  

^a Baker Laboratory   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CATALYSIS; CHEMICAL ACTIVATION; DIMERS; ENZYMES; FLUORESCENCE; METABOLISM; OLIGOMERS;

ALLOSTERIC ACTIVATOR; ALLOSTERIC INHIBITOR; BINDING AFFINITIES; CONFORMATIONAL CHANGE; FLUORESCENCE ENHANCEMENT; INORGANIC PHOSPHATES; MITOCHONDRIAL ENZYMES; TRYPTOPHAN FLUORESCENCE;

BINS;

BIS 2 (5 PHENYLACETAMIDO 1,2,4 THIADIAZOL 2 YL)ETHYL SULFIDE; ENZYME INHIBITOR; GLUTAMINASE; GLUTAMINASE C; PHENYLALANINE; PHOSPHATE; SULFATE; TRYPTOPHAN; UNCLASSIFIED DRUG; BENZENEACETAMIDE DERIVATIVE; BIS-2-(5-PHENYLACETAMIDO-1,2,4-THIADIAZOL-2-YL)ETHYL SULFIDE; CB-839; ENZYME ACTIVATOR; MITOCHONDRIAL PROTEIN; SULFIDE; THIADIAZOLE DERIVATIVE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIMERIZATION; DRUG EFFECT; ENZYME ACTIVATION; ENZYME BINDING; ENZYME DEGRADATION; ENZYME STRUCTURE; FLUORESCENCE; MOUSE; NONHUMAN; AGONISTS; ALLOSTERISM; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; GENETICS; MISSENSE MUTATION; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; ANIMALS; BENZENEACETAMIDES; ENZYME ACTIVATORS; ENZYME INHIBITORS; GLUTAMINASE; MICE; MITOCHONDRIAL PROTEINS; MUTATION, MISSENSE; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; SULFIDES; THIADIAZOLES;

EID: 85018484835     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.758219     Document Type: Article

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