Heavy riboflavin synthase of Bacillus subtilis. Primary structure of the beta subunit.
Article Details
- CitationCopy to clipboard
Ludwig HC, Lottspeich F, Henschen A, Ladenstein R, Bacher A
Heavy riboflavin synthase of Bacillus subtilis. Primary structure of the beta subunit.
J Biol Chem. 1987 Jan 25;262(3):1016-21.
- PubMed ID
- 3100522 [ View in PubMed]
- Abstract
Heavy riboflavin synthase is a 1,000,000-Da protein catalyzing the last two reactions of riboflavin biosynthesis. The enzyme complex consists of 60 beta subunits (Mr = 16,200) and approximately three alpha subunits (Mr = 23,000). beta subunits were isolated and cleaved with cyanogen bromide. Fragments were isolated and further digested with trypsin and staphylococcal protease. Peptides were isolated by high performance liquid chromatography. Sequences were determined by automated liquid-phase Edman degradation. The complete sequence of the beta subunit (154 amino acids) was established by direct sequencing of the NH2 terminus, sequencing of overlapping peptides, and carboxypeptidase degradation of the COOH terminus. The sequence shows no detectable homologies to other proteins. A computer prediction of secondary structure elements indicates 34% alpha helix and 30% beta sheet.