2024
A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity
Zavala E, Dansereau S, Burke M, Lipchock J, Maschietto F, Batista V, Loria J. A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity. Protein Science 2024, 33: e5009. PMID: 38747379, PMCID: PMC11094782, DOI: 10.1002/pro.5009.Peer-Reviewed Original ResearchConceptsCatalytic activityPhenylphosphonic acidAnalysis of molecular dynamics trajectoriesNMR chemical shiftsSalt bridgesMolecular dynamics trajectoriesC-terminal carboxyl groupChemical shiftsCombination of solution NMRMolecular dynamicsGuanidinium moietyCarboxyl groupsPara-nitrophenylphosphateSolution NMRActive site inhibitorsHistidine phosphataseActive siteElectrostatic interactionsDynamics trajectoriesEnzymatic functionC-terminusGlycine residuesSubstrate affinityBiochemical experimentsBinding affinity
2009
Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase
Wang Y, Berlow RB, Loria JP. Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase. Biochemistry 2009, 48: 4548-4556. PMID: 19348462, PMCID: PMC2713366, DOI: 10.1021/bi9002887.Peer-Reviewed Original ResearchConceptsLoop 7Triosephosphate isomeraseLoop 6Chicken triosephosphate isomeraseC-terminal hingeActive site loopActive site loop motionArchaeal homologueEnzyme triosephosphate isomeraseMutant enzymesEnzymatic functionProtein sequencesBiological functionsSite loopEnzymatic activityFold lossTemperature-dependent NMR experimentsLoop motionModel systemIsomeraseSequenceActive siteEnzymeEnzymatic reactionsMutants