PMID:177283

Citation	Burr, B, Walker, J, Truffa-Bachi, P and Cohen, GN (1976) Homoserine kinase from Escherichia coli K12. Eur. J. Biochem. 62:519-26
Abstract	Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr = 60000) composed of apparently identical polypeptide chains (Mr = 29000). Its amino acid composition and N-terminal sequence have been determined. L-Threonine is a competitive inhibitor of the substrate L-homoserine; this inhibition is straighforward and shows no sign of co-operativity. Evidence is presented that homoserine and threonine bind to the same site of this non-allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acids/analysis; Binding Sites; Enzyme Activation/drug effects; Escherichia coli/enzymology; Homoserine; Kinetics; Macromolecular Substances; Magnesium/pharmacology; Molecular Weight; Peptide Fragments/analysis; Phosphotransferases/isolation & purification; Phosphotransferases/metabolism; Protein Binding; Spectrophotometry, Ultraviolet; Threonine/pharmacology
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