Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine.
A new simplified procedure for the purification of chorismate mutase/prephenate dehydratase, based on affinity chromatography on Sepharosyl-phenylalanine, has been developed. The method utilizes the effect of NaCl on the binding properties of the enzyme. NaCl inhibits both the mutase and dehydratase activities of the enzyme. In each case this inhibition is cooperative indicating homotropic interactions between NaCl binding sites on the enzyme. In addition NaCl induces homotropic cooperative effects between chorismate binding sites and between prephenate binding sites. NaCl also increases the sensitivity of the enzyme to inhibition by phenylalanine.
D001665:Binding Sites / Q000187:drug effects; D002827:Chorismic Acid / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods*; D004926:Escherichia coli / Q000201:enzymology; D006836:Hydro-Lyases / Q000302:isolation & purification*; D007700:Kinetics; D010649:Phenylalanine / Q000494:pharmacology; D011302:Prephenate Dehydratase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012965:Sodium Chloride / Q000494:pharmacology*
D012965:Sodium Chloride; D010649:Phenylalanine; D006836:Hydro-Lyases; D011302:Prephenate Dehydratase; D002827:Chorismic Acid