PMID:9753654

Citation	Wang, X, Deng, Z and Kemp, RG (1998) An essential methionine residue involved in substrate binding by phosphofructokinases. Biochem. Biophys. Res. Commun. 250:466-8
Abstract	An alignment of all PPi-dependent phosphofructokinases and all allosteric ATP-dependent PFKs shows relatively few residues that are fully conserved. One residue that is conserved is a methionine residue that appears from the crystal structure of Escherichia coli PFK to be interacting with fructose 6-P. Very conservative substitutions for this methionine with leucine or isoleucine by site-directed mutagenesis of E. coli ATP-PFK and Entamoeba histolytica PPi-PFK produced profound decreases either in the apparent affinity for fructose 6-P or in maximal velocity, or both. Methionine provides a highly specific interaction with fructose 6-P for binding and for transition state stabilization.
Links	PubMed Online version:10.1006/bbrc.1998.9311
Keywords	Allosteric Regulation; Animals; Binding Sites; Conserved Sequence; Entamoeba/enzymology; Escherichia coli/enzymology; Methionine; Mutation; Phosphofructokinase-1/chemistry; Phosphofructokinase-1/genetics; Phosphofructokinase-1/metabolism; Substrate Specificity
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