PMID:7575542

Citation	Zheng, RL and Kemp, RG (1995) Phosphofructo-1-kinase: role of charge neutralization in the active site. Biochem. Biophys. Res. Commun. 214:765-70
Abstract	Previous studies of Escherichia coli phosphofructo-1-kinase have shown that mutation of Asp 127 lowers kcat by 5 orders of magnitude. As shown here, introduction of a second mutation (R252Q) that neutralizes a positive charge in the active site increases activity of D127S by 100 fold, suggesting that part of the effect of the Asp mutation may be attributed to non-specific charge interactions. This conclusion is supported by the fact that the R252Q mutant shows a pH dependence that is the reverse of the wild type enzyme, whereas the double mutant has a pH dependence that resembles that of wild type enzyme, although somewhat attenuated.
Links	PubMed Online version:10.1006/bbrc.1995.2352
Keywords	Amino Acid Sequence; Aspartic Acid; Base Sequence; Binding Sites; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Phosphofructokinase-1/chemistry; Phosphofructokinase-1/metabolism; Point Mutation; Recombinant Proteins/metabolism
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