Table 5.

Mutated FMO3 showed different amino acids predicted for the TMA binding sites. Different haplotypes present in the mutated forms of FMO3 were predicted to change the aa characteristic of wild-type enzyme catalytic site, probably leading to an impairment of FMO3 activity. The “X” indicates that the specific aa in the related row is an integral part of the FMO3 active site when the variant/s reported in the columns is/are carried by the FMO3 gene.

	FMO3 Haplotypes
Active site a.a. Residues	Wild-Type	Y331Stop	P153L + E158K	P380Fs	P380Fs + E308G	P153L + E158K + P380Fs	E158K	V257M	E308G + E158K	R492W + E158K	R238Q + E158K	G475D + E158K	D141V + G180V	R238P + G475D
Gly 9				X	X	X
Ala 10				X	X	X
Gly 11				X	X	X
Val 12				X	X	X
Ser 13				X	X	X
Gly 14				X	X	X
Glu 32				X	X	X
Gly 38					X	X
Gly 39				X	X	X
Leu 40				X	X	X
Ala 52				X	X	X
Cys 146				X	X	X
Ser 147				X	X	X
Gly 148				X	X	X
Hys 149				X	X	X
Val 151					X	X
Ser 216	X							X
Gly 217	X							X
Ser 218	X							X
Trp 219	X							X
Gly 240		X
Leu 243		X
Lys 244		X
Leu 247		X
Ile 251		X
Ser 252		X
Asp 253		X
Leu 255		X
Tyr 256		X
Gln 259		X
Pro 273	X							X
Asn 275	X							X
Gly 276	X							X
Leu 278	X							X
Arg 279	X	X	X				X	X	X	X	X	X		X
Lys 280	X							X
Glu 281	X							X
Pro 282	X							X
Leu 352													X
Phe 353													X
Lys 354													X
Gly 355													X
Phe 371													X
Val 372													X
Ser 381				X	X	X
Lys 412			X				X		X	X	X	X	X	X
Met 413													X
Lys 415			X				X		X	X	X	X		X
Lys 416			X				X		X	X	X	X	X	X
Arg 417			X						X	X	X	X		X
Trp 419			X				X		X	X	X	X		X
Phe 420			X				X		X	X	X	X		X
Lys 422			X				X				X	X		X
Thr 425			X				X		X	X	X	X		X
Ile 426													X
Gln 427			X				X		X	X	X	X		X
Thr 428			X				X		X	X	X	X	X	X
Asp 429			X				X		X	X	X	X		X
Tyr 433													X