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- Title
A directed-overflow and damage-control N-glycosidase in riboflavin biosynthesis.
- Authors
Frelin, Océane; Huang, Lili; Hasnain, Ghulam; Jeffryes, James G.; Ziemak, Michael J.; Rocca, James R.; Bing Wang; Rice, Jennifer; Roje, Sanja; Yurgel, Svetlana N.; Gregory III, Jesse F.; Edison, Arthur S.; Henry, Christopher S.; de Crecy-Lagard, Valerie; Hanson, Andrew D.
- Abstract
Plants and bacteria synthesize the essential human micronutrient riboflavin (vitaminB2) via the same multi-step pathway. The early intermediates of this pathway are notoriously reactive and may be overproduced in vivo because riboflavin biosynthesis enzymes lack feedback controls. In the present paper, we demonstrate disposal of riboflavin intermediates by COG3236 (DUF1768), a protein of previously unknown function that is fused to two different riboflavin pathway enzymes in plants and bacteria (RIBR andRibA respectively).We present cheminformatic, biochemical, genetic and genomic evidence to show that: (i) plant and bacterial COG3236 proteins cleave the N-glycosidic bond of the first two intermediates of riboflavin biosynthesis, yielding relatively innocuous products; (ii) certain COG3236 proteins are in a multi-enzyme riboflavin biosynthesis complex that gives them privileged access to riboflavin intermediates; and (iii) COG3236 action in Arabidopsis thaliana and Escherichia coli helpsmaintain flavin levels. COG3236 proteins thus illustrate two emerging principles in chemical biology: directed overflow metabolism, in which excess flux is diverted out of a pathway, and the preemption of damage from reactive metabolites.
- Subjects
GLYCOSIDASES; RIBOFLAVIN synthase; VIBRIO vulnificus; VITAMIN B2 metabolism; ARABIDOPSIS thaliana; ESCHERICHIA coli
- Publication
Biochemical Journal, 2015, Vol 466, Issue 1, p137
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BJ20141237