Identification of the Key Enzyme of Roseoflavin Biosynthesis. Issue 20 (9th April 2016)

• Record Type: Journal Article
• Authors: Schwarz, Julia; Konjik, Valentino; Jankowitsch, Frank; Sandhoff, Roger; Mack, Matthias
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 20(2016)
• Page Start: 6103
• Page End: 6106
• Publication Date: 2016-04-09
• Subjects: riboflavin -- riboflavin-5′-phosphate -- roseoflavin -- streptomyces davawensis; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201600581
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The bacteria Streptomyces davawensis and Streptomyces cinnabarinus produce roseoflavin, the only known natural riboflavin (vitamin B2 ) analogue with antibiotic activity. Roseoflavin can be considered a natural antimetabolite and has been postulated to be biosynthesized from riboflavin via the key intermediate 8‐demethyl‐8‐aminoriboflavin (AF). The required site‐specific substitution of one of the methyl groups on the dimethylbenzene ring of riboflavin by an amino group (to give AF) is challenging. The pathway from riboflavin to AF has remained elusive, and the corresponding enzyme/s was/were unknown. Herein, we show by systematic gene deletion, heterologous gene expression, and biochemical studies that the enzyme specified by the gene BN159_7989 from S. davawensis is able to carry out a whole set of chemical reactions starting from riboflavin‐5′‐phosphate to give the final product 8‐demethyl‐8‐aminoriboflavin‐5′‐phosphate (AFP). Abstract : All by myself : Unexpectedly, a single enzyme (RosB) was found to catalyze several essential steps of the biosynthesis of the antibiotic roseoflavin from riboflavin (vitamin B2). RosB was identified in the bacterium Streptomyces davawensis, which was used to produce roseoflavin in a bioreactor containing a nutrient broth.