2012
Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB
Yu T, Mok K, Kennedy K, Valton J, Anderson K, Walker G, Taga M. Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB. Protein Science 2012, 21: 839-849. PMID: 22528544, PMCID: PMC3403419, DOI: 10.1002/pro.2068.Peer-Reviewed Original ResearchConceptsConserved residuesFlavin mononucleotideReduced catalytic functionPurified mutant proteinsBacterium Sinorhizobium melilotiActive site residuesReduced flavin mononucleotideFlavin isoalloxazine ringCatalytic residuesMutant proteinsFlavin bindingDMB synthesisStructure-function relationshipsActive siteEnzyme familyGenetic screeningSite residuesMutant formsLower axial ligandBound flavinCatalytic functionMutantsEnzyme assaysIsoalloxazine ringBluB
2000
Energetics of S-Adenosylmethionine Synthetase Catalysis †
McQueney M, Anderson K, Markham G. Energetics of S-Adenosylmethionine Synthetase Catalysis †. Biochemistry 2000, 39: 4443-4454. PMID: 10757994, DOI: 10.1021/bi992876s.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceBinding SitesCatalysisComputer SimulationDiphosphatesEscherichia coliFluorescenceHydrolysisIsomerismKineticsLigandsMethionineMethionine AdenosyltransferaseOxygenOxygen IsotopesPhosphatesPolyphosphatesS-AdenosylmethionineSolventsThermodynamicsTitrimetryWaterConceptsFree energy profilesSubstrate bindingLoop movementEnergy profilesFormation of AdoMetS-adenosylmethionineChemical interconversion stepPre-steady-state kineticsS-adenosylmethionine synthetaseProduct releaseP(i) complexEquilibrium binding measurementsEnzyme-catalyzed reactionsAdoMet formationBiological alkylating agentsConcentration of substrateFormation reactionCrystallographic studiesEnzyme turnoverEquilibrium constantsCatalyze formationRate constantsInterconversion stepActive siteBinding energy
1997
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Munson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.Peer-Reviewed Original Research