Cover Picture: Catalysis of an Essential Step in Vitamin B2 Biosynthesis by a Consortium of Broad Spectrum Hydrolases (ChemBioChem 17/2015). Issue 17 (November 2015)

• Record Type: Journal Article
• Authors: Sarge, Sonja; Haase, Ilka; Illarionov, Boris; Laudert, Dietmar; Hohmann, Hans‐Peter; Bacher, Adelbert; Fischer, Markus
• Is Part Of: Chembiochem. Volume 16:Issue 17(2015)
• Page Start: 2405
• Page End: 2405
• Publication Date: 2015-11
• Subjects: biosynthesis -- haloacid dehalogenase -- hydrolases -- isoenzymes -- vitamin B2; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201500578
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The cover picture shows the biosynthesis of riboflavin. Enzymes of B. subtilis involved in this pathway are indicated and the enzymes identified for the first time in this paper (YcsE, YitU and YwtE) are highlighted. The left corner shows a dendrogram of the HAD‐like proteins of B. subtilis studied in this work. Three HAD members were found to dephosphorylate 5‐amino‐6‐ribitylamino‐2, 4(1 H, 3 H )‐pyrimidinedione 5'‐phosphate (ARP‐P) at rates ≥0.7 µmol mg −1 min −1 with KM values in the double‐digit µM range. Several others catalyse the reaction at lower rates. B. subtilis proteins that catalyse the hydrolysis of ARP‐P can also catalyse the hydrolysis of FMN at similar or higher respective rates. Notably, YitU dephosphorylates FMN at a rate of about 17 µmol mg −1 min −1, about 10 times faster than ARP‐P. More details can be found in the Communication by M. Fischer et al. onpage 2466 in Issue 17, 2015 (DOI:10.1002/cbic.201500352 ).