2.1.1.267	D168L	isoform ROMT-15, complete loss of activity	700855	
2.1.1.267	D168L	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	D194L	isoform ROMT-15, complete loss of activity	700855	
2.1.1.267	D194L	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	D209L	isoform ROMT-17, complete loss of activity	700855	
2.1.1.267	D209L	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	D234L	isoform ROMT-17, complete loss of activity	700855	
2.1.1.267	D234L	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	E112L	isoform ROMT-17, 14% loss of activity	700855	
2.1.1.267	E112L	mutation results in 40% loss of activity (with quercetin as substrate)	700855	
2.1.1.267	E69L	isoform ROMT-15, 14% loss of activity	700855	
2.1.1.267	E69L	mutation results in 14% loss of activity (with quercetin as substrate)	700855	
2.1.1.267	G13E	site-directed mutagenesis, the mutant shows increased activity compared to wild-type	757323	
2.1.1.267	L87A	site-directed mutagenesis, the mutant shows highly decreased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-L87R mutant is equal to that of Paeonia tenuifolia PtAOMT wild-type	757323	
2.1.1.267	L87R	site-directed mutagenesis, the mutant shows highly decreased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-L87R mutant is equal to that of Paeonia tenuifolia PtAOMT wild-type	757323	
2.1.1.267	additional information	construction of a multifunctional flavonoid O-methyltransferase fusing tomato 3'-O-methyltransferase OMT3 and Oryza sativa naringenin 7-O-methyltransferase NOMT. The OMT3/NOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual OMT3 and NOMT. The OMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using OMT3/NOMT-transformed Escherichia coli generates corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-Omethyltaxifolin, respectively	757460	
2.1.1.267	additional information	flower color modification in Rosa hybrida by expressing the S-adenosylmethionine: anthocyanin 3',5'-O-methyltransferase gene from Torenia hybrida, phenotypes of T-DNA insertion transgenic plants, overview	757955	
2.1.1.267	additional information	generation of a multifunctional FOMT fusing a 3'-OMT (SlOMT3, EC 2.1.1.267) and a 7-OMT (OsNOMT, EC 2.1.1.82). The SlOMT3/OsNOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual SlOMT3 and OsNOMT. The SlOMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively, suggesting that the fusion enzyme can sequentially methylate flavonoids into di-O-methylflavonoids. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using SlOMT3/OsNOMT-transformed Escherichia coli generated corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-O-methyltaxifolin, respectively. These results indicate that dimethoxyflavonoids may be efficiently produced from non-methylated flavonoid precursors through a one-step biotransformation using the engineered Escherichia coli harboring the SlOMT3/OsNOMT fusion gene	757460	
2.1.1.267	additional information	silencing of AnthOMT in hypocotyl tissue, several hypocotyls of three lines (57, 85 and 87) show an anthocyanin profile that is different to that of the wild-type, and show a strong reduction in malvidin-type anthocyanins, while other lines (64, 66 and 71) show only wild-type anthocyanin profiles	736999	
2.1.1.267	N195I	isoform ROMT-15, complete loss of activity	700855	
2.1.1.267	N195I	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	N235I	isoform ROMT-17, complete loss of activity	700855	
2.1.1.267	N235I	mutation abolishes activity (with quercetin as substrate)	700855	
2.1.1.267	R87L	site-directed mutagenesis, the mutant shows highly increased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-R87L mutant is equal to that of Paeonia suffruticosa PsAOMT wild-type	757323	
2.1.1.267	T205R	site-directed mutagenesis, the mutant shows increased activity compared to wild-type	757323	
2.1.1.267	T85A	site-directed mutagenesis, the mutant shows increased activity compared to wild-type	757323