The Claim
Mutation of the selenocysteine residue at position 266 in human type 2 deiodinase to cysteine or a stop codon reduces selenium-75 incorporation in transfected HEK-293 cells without altering the enzyme's deiodination activity, indicating that this residue is not essential for catalytic function under in vitro conditions.
What the research says
Supports is higher
Support is ahead, but a single strong opposing study can change this.
These are independent scores, not a percentage. Higher-grade studies count more, so a single strong opposing study can outweigh several weaker ones.
Changing a specific amino acid in the human type 2 deiodinase enzyme reduces its ability to take up selenium-75 in laboratory-grown human cells, but does not change its ability to remove iodine from thyroid hormones, suggesting this amino acid is not required for the enzyme's core function in this setting.
See the scientific wording
Mutation of the selenocysteine residue at position 266 in human type 2 deiodinase to cysteine or a stop codon reduces selenium-75 incorporation in transfected HEK-293 cells without altering the enzyme's deiodination activity, indicating that this residue is not essential for catalytic function under in vitro conditions.
What the research says
1 studyScientists changed a tiny part of an enzyme that uses selenium, and while the enzyme no longer grabbed selenium as well, it still worked fine at doing its job. So that part isn’t needed for the enzyme to function.
Score breakdown, mechanism chain, raw evidence, ideal studies needed & 1 supporting studies
Not medical advice. For informational purposes only. Always consult a qualified healthcare professional before making health decisions.