2.5.1.9	A43L	decrease in affinity for substrate 6,7-dimethyl-8-ribityllumazine. A43L replacement causes substantial perturbation of the overall binding site topology	687468	
2.5.1.9	C48A	site-directed mutagenesis, nearly inactive mutant	658346	
2.5.1.9	C48M	site-directed mutagenesis, nearly inactive mutant	658346	
2.5.1.9	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	687468	
2.5.1.9	C48S	site-directed mutagenesis, highly decreased activity compared to the wild-type enzyme	658346	
2.5.1.9	D143G	site-directed mutagenesis, soluble protein, too unstable to be purified	637580	
2.5.1.9	D143N	site-directed mutagenesis, soluble protein, too unstable to be purified	637580	
2.5.1.9	D185L	site-directed mutagenesis, low remaining activity	637580	
2.5.1.9	DELTA1-180	variant that lacks the C-terminal extension the coiled-coil and C-terminal peptide (AaRS1-180)	759481	
2.5.1.9	DELTA1-196	variant that lacks the C-terminal extension (1-196). Substantial decrease in association efficiency with lumazine synthase is observed for the truncated variant	759481	
2.5.1.9	DELTA180-196	variant that lacks the C-terminal extension the coiled-coil segment (DELTA180-196). The mutant enzyme associated with lumazine synthase to an about 3fold higher extent than the full-length riboflavin synthase	759481	
2.5.1.9	E183G	site-directed mutagenesis, reduced activity	637580	
2.5.1.9	E66G	site-directed mutagenesis, low remaining activity	637580	
2.5.1.9	E85G	site-directed mutagenesis, reduced activity	637580	
2.5.1.9	F2A	nearly inactive mutant, comparison of kinetics for wild-type and mutant enzymes	658235	
2.5.1.9	F2A	site-directed mutagenesis, no remaining activity	637580	
2.5.1.9	F2Y	site-directed mutagenesis, very low remaining activity	637580	
2.5.1.9	H102Q	highly reduced activity compared to the wild-type enzyme, comparison of kinetics for wild-type and mutant enzymes	658235	
2.5.1.9	H102Q	site-directed mutagenesis, very low remaining activity	637580	
2.5.1.9	H97Q	site-directed mutagenesis, low remaining activity	637580	
2.5.1.9	K137A	site-directed mutagenesis, low remaining activity	637580	
2.5.1.9	additional information	5 mutants genes cannot be expressed recombinantly in Escherichia coli: C48S, T50R, T67R, T148R, T165R	637580	
2.5.1.9	additional information	a F2DELTA deletion mutant construct has no remaining activity	637580	
2.5.1.9	additional information	overexpression in Escherichia coli can suppress the lack of pyrimidine deaminase/reductase in a riboflavin-deficient ribD- strain	684754	
2.5.1.9	additional information	recombinant sequence segment 1-97 forms a homodimer that can bind riboflavin, 6,7-dimethyl-8-ribityllumazine, and trifluoromethyl-substituted 8-ribityllumazine derivatives, and is required for ligand binding, recombinant sequence segment 101-213 is unstable and only partially involved in riboflavin binding	637583	
2.5.1.9	N181G	site-directed mutagenesis, soluble protein, too unstable to be purified	637580	
2.5.1.9	N45G	site-directed mutagenesis, slightly reduced activity	637580	
2.5.1.9	N83G	site-directed mutagenesis, reduced activity	637580	
2.5.1.9	S146A	site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme	658346	
2.5.1.9	S146C	site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme	658346	
2.5.1.9	S146G	site-directed mutagenesis, low remaining activity	637580	
2.5.1.9	S41A	site-directed mutagenesis, mutant produces a dimeric pentacyclic reaction intermediate, i.e. compound Q, which can be cleaved in 2 different ways by the enzyme	657905	
2.5.1.9	S41A	site-directed mutagenesis, very low remaining activity	637580	
2.5.1.9	T3R	site-directed mutagenesis, slightly reduced activity, low expression rate	637580	
2.5.1.9	T50A	production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude	704202	
2.5.1.9	T67A	production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude	704202	
2.5.1.9	T71A	site-directed mutagenesis, slightly reduced activity	637580	
2.5.1.9	W207A	the mutant enzyme is taken up by lumazine synthase only 30% less efficiently than wild-type enzyme	759481	
2.5.1.9	Y133A	site-directed mutagenesis, soluble protein, too unstable to be purified	637580