1.5.1.5	C58Y	kcat/Km for 5,10-methenyltetrahydrofolate is 8.4fold lower than wild-type value	744335	
1.5.1.5	D121A	kcat/Km for 5,10-methenyltetrahydrofolate is 600fold lower than wild-type value	744335	
1.5.1.5	D133E	mutant retains no dehydrogenase activity	701402	
1.5.1.5	D133E	no dehydrogenase activity retained, Mg2+ binding site	701402	
1.5.1.5	G122D	kcat/Km for 5,10-methenyltetrahydrofolate is 84fold lower than wild-type value	744335	
1.5.1.5	K54S	kcat/Km for 5,10-methenyltetrahydrofolate is identical to wild-type value	744335	
1.5.1.5	K56Q/Q100K	retaines two-third of dehydrogenase activity but no cyclohydrolase activity	701402	
1.5.1.5	K56Q/Q100K	site-directed mutagenesis shows that the double mutant has no cyclohydrolase activity but retains two-thirds of the normal dehydrogenase activity	701402	
1.5.1.5	additional information	asparagine-125 is required for folate-substrate binding, arginine-173 mutation causes 500fold increase in the Km for NADP, serine-197 mutation a 20fold increase	701402	
1.5.1.5	additional information	knockout mutant of MTHFD2 is embryonic lethal in mice at about 12 days gestation, no normal development of hematogenesis in the liver	701402