Journal article

THE SELF-ASSOCIATION OF CHORISMATE MUTASE-PREPHENATE DEHYDRATASE FROM ESCHERICHIA-COLI-K12

GS BALDWIN, GH MCKENZIE, BE DAVIDSON

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS | Published : 1981

Abstract

The state of association of chorismate mutase/prephenate dehydratase (EC 5.4.99.5/ 4.2.1.51) from E. coli K12 has been studied using ultracentrifugal techniques. The smallest species inferred is a dimer of molecular weight 73,000-84,000, with a s20,w0 of 5.02 S at pH 8.2, I = 0.013 M. This species undergoes a concentration-dependent self-association which results in an equilibrium mixture of dimer, tetramer, and probably octamer, with a Mr of 164,000 at an enzyme concentration of 8.0 mg/ml under the same conditions. Addition of the feedback inhibitor phenylalanine (2 mm) or increase in ionic strength (I = 0.40 M), or a decrease in pH to 7.4 displaces this equilibrium toward the higher-molecu..

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