PMID:21878632
| Citation |
Brammer, LA, Smith, JM, Wade, H and Meyers, CF (2011) 1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism. J. Biol. Chem. 286:36522-31 |
|---|---|
| Abstract |
Emerging resistance of human pathogens to anti-infective agents make it necessary to develop new agents to treat infection. The methylerythritol phosphate pathway has been identified as an anti-infective target, as this essential isoprenoid biosynthetic pathway is widespread in human pathogens but absent in humans. The first enzyme of the pathway, 1-deoxy-D-xylulose 5-phosphate (DXP) synthase, catalyzes the formation of DXP via condensation of D-glyceraldehyde 3-phosphate (D-GAP) and pyruvate in a thiamine diphosphate-dependent manner. Structural analysis has revealed a unique domain arrangement suggesting opportunities for the selective targeting of DXP synthase; however, reports on the kinetic mechanism are conflicting. Here, we present the results of tryptophan fluorescence binding and kinetic analyses of DXP synthase and propose a new model for substrate binding and mechanism. Our results are consistent with a random sequential kinetic mechanism, which is unprecedented in this enzyme class. |
| Links |
PubMed PMC3196101 Online version:10.1074/jbc.M111.259747 |
| Keywords |
Aldose-Ketose Isomerases/chemistry; Aldose-Ketose Isomerases/genetics; Aldose-Ketose Isomerases/metabolism; Catalysis; Drug Resistance, Bacterial/physiology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Humans; Kinetics; Models, Chemical; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Oxidoreductases/chemistry; Oxidoreductases/genetics; Oxidoreductases/metabolism; Protein Structure, Tertiary |
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