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Article

Complex structure of Bacillus subtilis RibG: the reduction mechanism during riboflavin biosynthesis.

The Journal of biological chemistry - 16 Jan 2009

Chen Sheng-Chia, Lin Yu-Hsin, Yu Hui-Chia, Liaw Shwu-Huey

Abstract excerpt

Bacterial RibG is a potent target for antimicrobial agents, because it catalyzes consecutive deamination and reduction steps in the riboflavin biosynthesis. In the N-terminal deaminase domain of Bacillus subtilis RibG, structure-based mutational analyses demonstrated that Glu51 and Lys79 are essential for the deaminase activity. In the C-terminal reductase domain, the complex structure with the substrate at...

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Source

Identifiers

PMID: 18986985
DOI: 10.1074/jbc.M805820200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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