2003
Detection and characterization of enzyme intermediates: utility of rapid chemical quench methodology and single enzyme turnover experiments
Anderson K. Detection and characterization of enzyme intermediates: utility of rapid chemical quench methodology and single enzyme turnover experiments. 2003, 19-48. DOI: 10.1093/oso/9780198524946.003.0002.Peer-Reviewed Original ResearchEnzyme active siteEnzyme intermediateProtein structure-function studiesSteady-state kinetic studiesStructure-function studiesTransient kinetic approachActive siteMolecule of substrateEnzyme catalysisQuenching methodologyEnzymeTurnover experimentsTransient kinetic techniquesStructure-based drug designEnzyme Transition StatesDrug designMechanistic informationKinetic techniquesSubstrate(sMillisecond time scaleProteinSitesPathwayKinetic studiesIntermediate
1998
Catalytic Mechanism of Kdo8P Synthase: Transient Kinetic Studies and Evaluation of a Putative Reaction Intermediate †
Liang P, Lewis J, Anderson K, Kohen A, D'Souza F, Benenson Y, Baasov T. Catalytic Mechanism of Kdo8P Synthase: Transient Kinetic Studies and Evaluation of a Putative Reaction Intermediate †. Biochemistry 1998, 37: 16390-16399. PMID: 9819231, DOI: 10.1021/bi981374w.Peer-Reviewed Original ResearchConceptsTransient kinetic studiesKDO8P synthaseRapid chemical quench experimentsIntermediate 2Chemical quench experimentsKinetic studiesBeta-pyranose formPutative reaction intermediatesChemical synthesisNMR spectroscopySynthetic 2Anomeric phosphatesReaction intermediatesCatalytic pathwayReaction pathwaysEnzyme catalysisCatalytic mechanismTurnover conditionsMechanistic pathwaysPutative reactionsReactionPhosphate hydrolysisSubstrate activityCorresponding control experimentsAlternate substrates