BY RON MAGOLDA
Medical Products Department
E.I. Du Pont de Nemours & Co.
Wilmington, Del.
G-binding proteins have been implicated in a variety of biological processes. A structural analysis of this interesting class of proteins has been presented. P.Woolley, B.F.C. Clark, “Homologies in the structures of G-binding proteins: an analysis based on elongation factor EF-Tu,” BioTechnology, 7, 9 13-20, September 1989. (Aarhus University, Arhus, Denmark).
The biosynthesis of the antibiotic thiostrepton presented several structural and biochemical challenges, which this communication overcomes.
·P. Zhou, D. O’Hagan, U. Mocek, Z. Zeng, L.-D. Yuen, et al., “Biosynthesis of the antibiotic thiostrepton, methylation of tryptophan in the formation of the quinaldic acid moiety by transfer of the methionine methyl group with net retention of configuration,” Journal of the American Chemical Society, 111, 7274-6, 30 August 1989. (University of Washington, Seattle; Ohio State University, Columbus; Los Alamos National Laboratory, N.Mex.)
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