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