2004
Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †
Wang C, Zakharova E, Li J, Joyce C, Wang J, Konigsberg W. Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †. Biochemistry 2004, 43: 3853-3861. PMID: 15049692, DOI: 10.1021/bi0302292.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBacteriophage T4Base Pair MismatchDNA Polymerase IDNA-Directed DNA PolymeraseEnzyme ActivationExodeoxyribonucleasesGlutamineHydrogen-Ion ConcentrationKineticsMutagenesis, Site-DirectedPhosphatesPhosphorylationProtein Structure, TertiaryRNA EditingSubstrate SpecificityT-PhagesThionucleotidesViral ProteinsConceptsRate-determining stepDivalent metal ionsPH-activity profileB family replicative DNA polymerasesChemical stepMetal ionsSingle-turnover conditionsWild-type enzymeEffects of pHKlenow fragmentB-family DNA polymerasesFamily DNA polymerasesState kineticsDNA polymeraseThree-dimensional structureDomain mutantsExonuclease reactionExonuclease activityPhosphorothioate linkagesPhi29 DNA polymeraseElemental effectsReplicative DNA polymerasesRepair DNA polymerasesExo activityCatalysis
1999
New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond
Porankiewicz J, Wang J, Clarke A. New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond. Molecular Microbiology 1999, 32: 449-458. PMID: 10320569, DOI: 10.1046/j.1365-2958.1999.01357.x.Peer-Reviewed Original ResearchConceptsClp proteaseClpP proteinATP-dependent Clp proteaseClp/Hsp100Escherichia coliKey metabolic enzymesPrecise regulatory mechanismsChaperone subunitsPhotosynthetic organismsHigher plantsRegulatory subunitCellular processesHeptameric ringsHexameric ringThree-dimensional structureProteolytic subunitNew insightsRegulatory mechanismsProtein turnoverMetabolic enzymesFunctional importanceSubunitsProteaseRecent findingsProtein