The Claim
Deiodinase activity in human liver microsomes follows ping-pong kinetics with dithiothreitol as the required cofactor, indicating a two-step catalytic mechanism.
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.
In human liver microsomes, deiodinase enzymes process substrates through a two-step chemical reaction that requires dithiothreitol as a cofactor, following a ping-pong kinetic pattern.
See the scientific wording
Deiodinase activity in human liver microsomes follows ping-pong kinetics with dithiothreitol as the required cofactor, indicating a two-step catalytic mechanism.
A liver enzyme removes iodine atoms from thyroid hormones in two distinct chemical steps, using a helper molecule to transfer electrons. The enzyme first binds the hormone, removes one iodine atom, then binds the helper molecule to reset itself before removing a second iodine atom. This two-step process repeats without releasing the hormone until both iodines are removed.
What the research says
1 studyStudy: Deiodination of thyroid hormone by human liver.
This study found that the liver enzyme that breaks down thyroid hormones uses a two-step chemical process that needs a helper molecule called dithiothreitol — just like the claim said. It’s not a simple one-step reaction, but a more complex two-step one.
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.