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Updated: Jul 12, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
Published on: December 19, 2010
Zinc is an essential cofactor for type I isopentenyl diphosphate:dimethylallyl diphosphate isomerase
Christina N Carrigan1, C Dale Poulter
1Department of Chemistry, University of Utah, 315 South 1400 East, Salt Lake City, UT 84112, USA.
Abstract:
Isopentenyl diphosphate (IPP) isomerase catalyzes the interconversion of IPP and dimethylallyl diphosphate (DMAPP). This is an essential reaction in the mevalonate pathway for biosynthesis of isoprenoid compounds. A crystal structure of Escherichia coli type I IPP isomerase shows a his3glu2 octahedral metal binding site (Durbecq, V. et al. EMBO, 2001, 20, 1530-1537). A metal ion analysis of recombinant E. coli type I IPP isomerase purified from metal-free buffer or buffer containing 10 muM ZnCl2 and 10 muM MnCl2 indicated that the protein contained one atom of Zn2+ per molecule. The metal content and the activity of the enzyme did not change when dialyzed for 6 h against metal-free buffer but rapidly decreased upon dialysis against buffer containing o-phenanthroline. Structural and catalytic roles for Zn2+ are discussed.
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