Evidence for the Chemical Mechanism of RibB (3,4-Dihydroxy-2-butanone 4-phosphate Synthase) of Riboflavin Biosynthesis

Autor:	Nikola Kenjić, Kathleen M. Meneely, Daniel J. Wherritt, Melissa C. Denler, Timothy A. Jackson, Graham R. Moran, Audrey L. Lamb
Rok vydání:	2022
Předmět:	Riboflavin Synthase Colloid and Surface Chemistry Formates Riboflavin General Chemistry Intramolecular Transferases Biochemistry Butanones Catalysis Phosphates
Zdroj:	Journal of the American Chemical Society. 144:12769-12780
ISSN:	1520-5126 0002-7863
Popis:	RibB (3,4-dihydroxy-2-butanone 4-phosphate synthase) is a magnesium-dependent enzyme that excises the C4 of d-ribulose-5-phosphate (d-Ru5P) as formate. RibB generates the four-carbon substrate for lumazine synthase that is incorporated into the xylene moiety of lumazine and ultimately the riboflavin isoalloxazine. The reaction was first identified by Bacher and co-workers in the 1990s, and their chemical mechanism hypothesis became canonical despite minimal direct evidence. X-ray crystal structures of RibB typically show two metal ions when solved in the presence of non-native metals and/or liganding non-substrate analogues, and the consensus hypothetical mechanism has incorporated this cofactor set. We have used a variety of biochemical approaches to further characterize the chemistry catalyzed by RibB from
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58109c1345733e584a8fcee057a5f73f https://doi.org/10.1021/jacs.2c03376 Zobrazit plný text záznamu