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
2002
The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*
Bulock K, Beardsley G, Anderson K. The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*. Journal Of Biological Chemistry 2002, 277: 22168-22174. PMID: 11948179, DOI: 10.1074/jbc.m111964200.Peer-Reviewed Original ResearchConceptsCyclohydrolase reactionProduction of inosine monophosphateRelease of tetrahydrofolateSteady-state kinetic techniquesStopped-flow absorbanceBifunctional enzymeActive siteBifunctional proteinSubstrate channelingInosine 5'-monophosphateCyclohydrolaseEnzymatic activityChemotherapeutic targetEnzyme reaction pathwayInosine monophosphateKinetic mechanismFormyltransferaseProteinEnzymeKinetic analysisPathwayKinetic advantageKinetic evidenceKinetic techniquesRibonucleotides