The degree of enzyme thermolability ( assessed as residual activity after heat inactivation ) is much greater in 665TT individuals ( 18 22 % ) compared with 677CT ( 56 % ) and 677CC ( 66 67 % ).
2.
In studies of human recombinant MTHFR, the protein encoded by 677T loses its FAD cofactor three times faster than the wild-type protein . 5-Methyl-THF slows the rate of FAD release in both the wild-type and mutant enzymes, although it is to a much greater extent in the mutant enzyme . < ref name = " YamadaK2001Effects " / Low folate status with the consequent loss of FAD enhances the thermolability of the enzyme, thus providing an explanation for the normalised homocysteine and DNA methylation levels in folate-replete 677TT individuals.
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