2003
Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase*
Fan K, Wei P, Feng Q, Chen S, Huang C, Ma L, Lai B, Pei J, Liu Y, Chen J, Lai L. Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase*. Journal Of Biological Chemistry 2003, 279: 1637-1642. PMID: 14561748, PMCID: PMC7980035, DOI: 10.1074/jbc.m310875200.Peer-Reviewed Original ResearchConceptsSARS 3C-like proteinaseDrug designCoronavirus 3C-like proteinaseMixture of monomersHigh cleavage efficiencyEnzyme catalysisInhibitor designSecondary structure studiesEnzymatic specific activityStructure studiesNon-canonical residuesDimeric formPeptide substratesGel filtrationDimeric interfaceLiquid chromatography assaySubstrate specificityCleavage efficiencyEnzyme concentrationChromatography assayHydrophobic residuesP2 positionPeptidesCatalysisMonomers
2001
Occurrence of paradoxical or sustained control by an enzyme when overexpressed: necessary conditions and experimental evidence with regard to hepatic glucokinase
DE ATAURI P, ACERENZA L, KHOLODENKO B, DE LA IGLESIA N, GUINOVART J, AGIUS L, CASCANTE M. Occurrence of paradoxical or sustained control by an enzyme when overexpressed: necessary conditions and experimental evidence with regard to hepatic glucokinase. Biochemical Journal 2001, 355: 787-793. PMID: 11311143, PMCID: PMC1221796, DOI: 10.1042/bj3550787.Peer-Reviewed Original ResearchConceptsRegulatory proteinsFlux control coefficientsParadoxical controlHigh flux control coefficientAllosteric enzymePathway fluxHepatic glucokinaseEnzymeEnzyme activitySigmoidal kineticsEnzyme kineticsControl coefficientsProteinEnzyme increasesGlucokinaseHill coefficientSubstrate concentrationEnzyme concentration
2000
Engineering a Living Cell to Desired Metabolite Concentrations and Fluxes: Pathways with Multifunctional Enzymes
Kholodenko B, Westerhoff H, Schwaber J, Cascante M. Engineering a Living Cell to Desired Metabolite Concentrations and Fluxes: Pathways with Multifunctional Enzymes. Metabolic Engineering 2000, 2: 1-13. PMID: 10935931, DOI: 10.1006/mben.1999.0132.Peer-Reviewed Original ResearchConceptsMultifunctional enzymeRest of metabolismMetabolic engineeringMetabolic control analysisCellular pathwaysCellular metabolismMolecular geneticsCellular enzymesLiving cellsEnzymeMetabolismPathwayGeneticsMachineryMetabolic patternsEnzyme concentrationSingle intermediateModulationCellsMetabolite concentrationsPatterns
1995
Defining control coefficients in non-ideal metabolic pathways
Kholodenko B, Molenaar D, Schuster S, Heinrich R, Westerhoff H. Defining control coefficients in non-ideal metabolic pathways. Biophysical Chemistry 1995, 56: 215-226. PMID: 17023325, DOI: 10.1016/0301-4622(95)00039-z.Peer-Reviewed Original ResearchMetabolic pathwaysFlux control coefficientsHigh enzyme concentrationsMetabolic control analysisBiochemical pathwaysElemental stepsMetabolite channellingMetabolic channellingRelevant pathwaysEnzyme activityPathwayEnzymeControl coefficientsEnzyme concentrationMoiety-conserved cyclesEqual modulationsSpeciesReverse rateElemental processesModulationActivityHow to reveal various aspects of regulation in group-transfer pathways
Kholodenko B, Westerhoff H. How to reveal various aspects of regulation in group-transfer pathways. Biochimica Et Biophysica Acta (BBA) - Bioenergetics 1995, 1229: 275-289. DOI: 10.1016/0005-2728(95)00013-9.Peer-Reviewed Original ResearchGroup-transfer pathwaysEnzyme-enzyme complexPathway componentsGene expressionMetabolic pathwaysAspects of regulationGenetic modulationSpecific inhibitorSuch inhibitorsEnzyme concentrationNon-competitive inhibitorEnzymeControl coefficientsPathwayIntact systemInhibitorsInhibited enzymeRegulationExpression
1993
The sum of the control coefficients of all enzymes on the flux through a group‐transfer pathway can be as high as two
van DAM K, van der VLAG J, KHOLODENKO B, WESTERHOFF H. The sum of the control coefficients of all enzymes on the flux through a group‐transfer pathway can be as high as two. The FEBS Journal 1993, 212: 791-799. PMID: 8462550, DOI: 10.1111/j.1432-1033.1993.tb17720.x.Peer-Reviewed Original ResearchConceptsGroup-transfer pathwaysReaction activityDissociation rate constantsElectron transfer chainAcceptor couplesEnzyme-enzyme interactionsEnzyme concentrationRate constantsEnzyme-enzyme complexEnzyme interactionsComplexesControl of enzymesEnzyme complexEnzymeConcentrationBacterial phosphoenolpyruvateMain pathwayInteractionConstantsChainControl analysisSimple metabolic pathwaysSugar phosphotransferase systemMultiplicity of Control
Westerhoff H, Jensen P, van der Gugten A, Kahn D, Kholodenko B, Schuster S, Oldenburg N, van Dam K, van Heeswijk W. Multiplicity of Control. 1993, 263-268. DOI: 10.1007/978-1-4615-2962-0_41.Peer-Reviewed Original Research
1988
A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics.
Anderson K, Sikorski J, Johnson K. A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics. Biochemistry 1988, 27: 7395-406. PMID: 3061457, DOI: 10.1021/bi00419a034.Peer-Reviewed Original ResearchConceptsPhosphoenol pyruvateBurst of product formationPre-steady-state burstQuantitation of reaction productsTransient-state kinetic analysisEnzyme-bound intermediateShikimate 3-phosphateSingle turnover experimentsPre-steady-stateSubstrate trapping experimentsRelease of substratesEquilibrium constantsSynthase reactionExcess enzymeBinding rateAbsence of phosphatePyruvateReverse reactionEnzymeTurnover experimentsEnzymatic reactionsKinetic competenceEnzyme concentrationFormation of productsConcentration of phosphate
1976
Inactivation of pyridoxal phosphate dependent enzymes by mono- and polyhaloalanines.
Silverman R, Abeles R. Inactivation of pyridoxal phosphate dependent enzymes by mono- and polyhaloalanines. Biochemistry 1976, 15: 4718-23. PMID: 974085, DOI: 10.1021/bi00666a028.Peer-Reviewed Original ResearchConceptsPyridoxal phosphate dependent enzymesDependent enzymesGamma-elimination reactionActive siteAlanine racemaseGlutamate-pyruvateCovalent modificationMechanism of inactivationEnzymeEnzyme concentrationInactivationCovalent labelingSchiff base formationRate of inactivationPyridoxalGamma-cystathionaseBetaActivated Michael acceptorsBase formationMichael acceptorsMichael addition
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