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Volume 271, Number 52, Issue of December 27, 1996 pp. 33201-33207
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Biosynthesis of Riboflavin
LUMAZINE SYNTHASE OF ESCHERICHIA COLI

(Received for publication, May 3, 1996, and in revised form, August 13,1996)

From the Department of Chemistry, Technical University of Munich, Lichtenbergstrasse 4, D-85747 Garching, Federal Republic of Germany

A gene located at 443 kilobases on the Escherichia coli chromosome (subsequently designated ribE) was expressed in a recombinant E. coli strain and was shown to code for the enzyme 6,7-dimethyl-8-ribityllumazine synthase. The recombinant enzyme was purified to homogeneity. The protein is an icosahedral capsid of 60 subunits with a mass of about 1 MDa as shown by hydrodynamic studies and by electron microscopy. In contrast to the icosahedral lumazine synthase-riboflavin synthase complex of Bacillus subtilis, the lumazine synthase of E. coli is not physically associated with another enzyme of the riboflavin pathway, and the core of the icosahedral capsid is empty. The RIB4 gene of Saccharomyces cerevisiae was also expressed to a high level (about 40% of cellular protein) in E. coli. The recombinant protein is a pentamer of 90 kDa. An insertion of 4 amino acids into helix ₄ is likely to hinder the formation of an icosahedral capsid by the yeast protein. The kinetic properties of lumazine synthase of E. coli, B. subtilis, and S. cerevisiae are similar.

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