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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase.

Escherichia coli grown in limited methionine and excess norleucine media accumulate cyanogen bromide-resistant species of proteins after the methionine supply is exhausted. Bacteria, transformed by recombinant plasmid pIPD37 carrying the adk gene and grown under limiting methionine and excess norleucine, synthesize 16-20% of adenylate kinase molecules having all 6 methionine residues replaced by norleucine. Species showing only partial replacement of methionine residues by norleucine are identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after cyanogen bromide treatment of pure enzyme. Norleucine-substituted adenylate kinase shows structural and catalytic properties similar to the wild-type protein as indicated by circular dichroism spectroscopy and kinetic experiments but exhibits a much higher resistance to hydrogen peroxide inactivation under denaturing conditions.[1]


  1. Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase. Gilles, A.M., Marlière, P., Rose, T., Sarfati, R., Longin, R., Meier, A., Fermandjian, S., Monnot, M., Cohen, G.N., Bârzu, O. J. Biol. Chem. (1988) [Pubmed]
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