2003
Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis
Yoon J, Oh B, Kim K, Park JE, Wang J, Kim HS, Kim Y. Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis. Biochemical And Biophysical Research Communications 2003, 310: 651-659. PMID: 14521961, DOI: 10.1016/j.bbrc.2003.09.056.Peer-Reviewed Original ResearchConceptsCyclic amidasesD-hydantoinaseCatalytic propertiesHydrophobic interaction domainCatalytic activityEnzymatic catalysisHydrophobic interactionsCyclic ureidesReversible hydrolysisDimeric formHydrophobic patchDimeric interactionsOligomeric stateSpecific activityTetramerKinetic propertiesCatalysisLow specific activityDihydropyrimidinesPropertiesHydantoinsDimersDihydroorotaseHydrolysisInteraction
1999
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin
Silvian L, Wang J, Steitz T. Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin. Science 1999, 285: 1074-1077. PMID: 10446055, DOI: 10.1126/science.285.5430.1074.Peer-Reviewed Original ResearchAcylationAdenosine MonophosphateAmino AcidsBinding SitesCrystallography, X-RayDNA-Directed DNA PolymeraseGlutamate-tRNA LigaseIsoleucineIsoleucine-tRNA LigaseModels, MolecularMupirocinNucleic Acid ConformationOligopeptidesProtein ConformationProtein Structure, SecondaryRNA, Transfer, GlnRNA, Transfer, IleStaphylococcus aureusSubstrate Specificity