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  • Title: Purification and characterization of 3-dehydroquinase from Escherichia coli.
    Author: Chaudhuri S, Lambert JM, McColl LA, Coggins JR.
    Journal: Biochem J; 1986 Nov 01; 239(3):699-704. PubMed ID: 2950851.
    Abstract:
    A procedure has been developed for the purification of 3-dehydroquinase from Escherichia coli. Homogeneous enzyme with specific activity 163 units/mg of protein was obtained in 19% overall yield. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 29,000. The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric. The catalytic properties of the enzyme have been determined and shown to be very similar to those of the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of Neurospora crassa.
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