Biosynthesis of riboflavin in Bacillus subtilis: function and genetic control of the riboflavin synthase complex.

Abstract:

:Two riboflavin synthase activities (heavy and light) have been observed in earlier studies with Bacillus subtilis. The heavy enzyme is a complex of one molecule of light enzyme (consisting of three alpha subunits) and approximately 60 beta subunits (A. Bacher, R. Bauer, U. Eggers, H. Harders, and H. Schnepple, p. 729--732, in T. P. Singer (ed.), Flavins and Flavoproteins, Elsevier, Amsterdam, 1976). The formation of alpha and beta subunits is coordinately controlled. Mutants apparently deficient in beta subunits were isolated as riboflavin requires after mutagenesis of B. subtilis with ICR 191. The mutants could grow with diacetyl instead of riboflavin. Growth with diacetyl was associated with the accumulation of substantial amounts of the riboflavin precursor, 6,7-dimethyl-8-(D-ribityl)lumazine. It follows that the mutants are deficient in an enzyme activity required for the formation of the lumazine from the pyrimidine precursor. We conclude that heavy riboflavin synthase is a bifunctional enzyme. The riboflavin synthase activity is mediated by the alpha subunits, whereas the beta subunits are necessary for an earlier biosynthetic step.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Bacher A,Mailänder B

doi

10.1128/JB.134.2.476-482.1978

subject

Has Abstract

pub_date

1978-05-01 00:00:00

pages

476-82

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

134

pub_type

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