Literature summary for 2.5.1.9 extracted from

Lee, C.Y.; Illarionov, B.; Woo, Y.E.; Kemter, K.; Kim, R.R.; Eberhardt, S.; Cushman, M.; Eisenreich, W.; Fischer, M.; Bacher, A.
Ligand binding properties of the N-terminal domain of riboflavin synthase from Escherichia coli (2007), J. Biochem. Mol. Biol., 40, 239-246.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
A43L	decrease in affinity for substrate 6,7-dimethyl-8-ribityllumazine. A43L replacement causes substantial perturbation of the overall binding site topology	Escherichia coli
C48S	mutation in the activity cavity, causes significant 19F NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein. Replacement of C48 changes the electron density topology in the N-terminal substrate binding site in the vicinity of C-6 and C-7 atoms of bound ligand	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)