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- W988472416 abstract "This chapter highlights assay, purification, and properties of heavy riboflavin synthase from Bacillus subtilis. Riboflavin synthase catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione from two molecules of 6,7-dimethyl-8-ribityllumazine. The formation of riboflavin from 6,7-dimethyl-8-ribityllumazine is monitored photometrically at 470 nm. One unit of enzyme activity catalyzes the formation of 1 nmol riboflavin/hr at 37°. The enzyme can be conveniently isolated from the genetically derepressed mutant H94 of Bacillus subtilis whose enzyme level is about 70-fold elevated as compared to the wild strain. Thus, the enzyme constitutes approximately 2% of the cellular protein. About 80% of the total activity in the crude extract corresponds to light enzyme. The enzyme is stable for periods of several months when stored as solution in 0.1 M phosphate (pH 7.0) containing 10 mM EDTA and 10 mM sodium sulfite. Well-ordered crystals have been obtained which yield X-ray reflections extending to a resolution of 3.5 Ǻ. Heavy riboflavin synthase dissociates in 0.1 M Tris buffer at pH values of ≥7, yielding trimers of α subunit which appear identical with light riboflavin synthase." @default.
- W988472416 created "2016-06-24" @default.
- W988472416 creator A5068798153 @default.
- W988472416 date "1986-01-01" @default.
- W988472416 modified "2023-10-12" @default.
- W988472416 title "[32] Heavy riboflavin synthase from Bacillus subtilis" @default.
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- W988472416 doi "https://doi.org/10.1016/0076-6879(86)22170-9" @default.
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