1.14.20.5	A120M	when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 162% of the catalytic activity relative to wild-type enzyme	742512	
1.14.20.5	F146I	when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 86% of the catalytic activity relative to wild-type enzyme	742512	
1.14.20.5	F146I/A120M	the enzyme activity of the double mutant is reduced to a level of about 10% of the activity of the wild type enzyme and the only product generated is apigenin	742512	
1.14.20.5	L311F	when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 355% of the catalytic activity relative to wild-type enzyme	742512	
1.14.20.5	L311F/A120M	the double mutant catalyzes the formation of 2-hydroxynaringenin and apigenin, although the ratio of these two compounds iss lower than that generated by the wild type enzyme	742512	
1.14.20.5	L311F/F146I	the double mutant catalyzes the formation of 2-hydroxynaringenin and apigenin, although the ratio of these two compounds iss lower than that generated by the wild type enzyme	742512	
1.14.20.5	L311F/F146I/A120M	the activity of the triple mutant falls to about 5% of the wild type enzyme	742512	
1.14.20.5	L311F/F146I/Y240P	inactive mutant	742512	
1.14.20.5	L311F/F146I/Y240P/A120M	inactive mutant	742512	
1.14.20.5	L311F/Y240P	the double mutant exhibits less flavone synthase activity than either the wild type or the Y240P single mutant enzymes	742512	
1.14.20.5	additional information	domain swapping experiments joining the N-terminus of flavanone 3beta-hydroxylase with the C-terminus of flavone synthase I and vice versa. Conversion of seven active site residues of flavanone 3beta-hydroxylase into the corresponding amino acids of flavone synthase I causes a nearly complete change in enzyme activity from flavanone 3beta-hydroxylase to flavone synthase I	689577	
1.14.20.5	additional information	gene DvFNS silencing by siRNA approach	726253	
1.14.20.5	additional information	transgenic seedlings of Arabidopsis thaliana accumulate substantial amounts of apigenin, and the apigenin level correlates with the abundance of enzyme mRNA	685694	
1.14.20.5	additional information	use of enzyme for construction of a system for producing unnatural flavonoids and stilbenes in Escherichia coli by expression of the respective genes on three plasmids. Incubation of the recombinant Escherichia coli with exogenously supplied carboxylic acids leads to production of 87 different polyketides, including 36 unnatural flavonoids and stilbenes	679173	
1.14.20.5	Y240P	the mutant enzyme converts naringenin to apigenin without producing any 2-hydroxynaringenin. The mutant has a higher affinity (lower Km) with naringenin than the wild type enzyme, but the catalytic efficiency of the mutant is lower than that of wild type enzyme. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 104% of the catalytic activity relative to wild-type enzyme	742512	
1.14.20.5	Y240P/A120M	the enzyme activity of the double mutant is reduced to a level of about 10% of the activity of the wild type enzyme and the only product generated is apigenin. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 175% of the catalytic activity relative to wild-type enzyme	742512	
1.14.20.5	Y240P/F146I	the enzyme activity of the double mutant is reduced to a level of about 10% of the activity of the wild type enzyme and the only product generated is apigenin	742512