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
2002
Crystal Structure of d-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity † , ‡
Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y. Crystal Structure of d-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity † , ‡. Biochemistry 2002, 41: 9410-9417. PMID: 12135362, DOI: 10.1021/bi0201567.Peer-Reviewed Original ResearchConceptsD-hydantoinaseExocyclic substituentsTIM-barrel foldStriking structural similarityApo crystal structureSubstrate recognitionBarrel foldCatalytic chemistryStructural comparisonSide-chain precursorBacillus stearothermophilusCrystal structureAmino acidsStructural similarityDihydroorotaseHydantoinsStereochemistrySubstituentsEnantioselectivityEnzymeStereospecific hydrolysisHydrolysisStructureChemistryHydantoinase