2002
The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*
Bulock K, Beardsley G, Anderson K. The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*. Journal Of Biological Chemistry 2002, 277: 22168-22174. PMID: 11948179, DOI: 10.1074/jbc.m111964200.Peer-Reviewed Original ResearchConceptsCyclohydrolase reactionProduction of inosine monophosphateRelease of tetrahydrofolateSteady-state kinetic techniquesStopped-flow absorbanceBifunctional enzymeActive siteBifunctional proteinSubstrate channelingInosine 5'-monophosphateCyclohydrolaseEnzymatic activityChemotherapeutic targetEnzyme reaction pathwayInosine monophosphateKinetic mechanismFormyltransferaseProteinEnzymeKinetic analysisPathwayKinetic advantageKinetic evidenceKinetic techniquesRibonucleotides
1997
Pre-steady state kinetic analysis of the bifunctional human amino-imidazole carboxamide ribonucleotide formyltransferase/AMP cyclohydrolase (AICARFT/IMPCHase), a 10-formyltetrahydro-folate-requiring enzyme essential for de novo purine biosynthesis
Rayl E, Moroson B, Beardsley G, Anderson K. Pre-steady state kinetic analysis of the bifunctional human amino-imidazole carboxamide ribonucleotide formyltransferase/AMP cyclohydrolase (AICARFT/IMPCHase), a 10-formyltetrahydro-folate-requiring enzyme essential for de novo purine biosynthesis. Clinical Biochemistry 1997, 30: 275-276. DOI: 10.1016/s0009-9120(97)87769-7.Peer-Reviewed Original Research