The Claim
The DIO1 p.Asn94Lys and p.Met201Ile variants reduce enzyme affinity for thyroxine, resulting in a two- to threefold increase in Michaelis constant (Km) and slower enzymatic velocity, as demonstrated by in vitro kinetic assays in transfected HEK293 cells.
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.
Two specific genetic changes in the DIO1 enzyme reduce its binding to thyroxine, leading to a two- to threefold higher Michaelis constant and reduced reaction speed in laboratory cell studies.
See the scientific wording
The DIO1 p.Asn94Lys and p.Met201Ile variants reduce enzyme affinity for thyroxine, resulting in a two- to threefold increase in Michaelis constant (Km) and slower enzymatic velocity, as demonstrated by in vitro kinetic assays in transfected HEK293 cells.
Changes in the DIO1 enzyme's structure make it harder for the enzyme to grab thyroxine, so it processes the hormone more slowly. This causes less active thyroid hormone to be made and more inactive hormone to build up in the blood.
What the research says
1 studyStudy: Human Type 1 Iodothyronine Deiodinase (DIO1) Mutations Cause Abnormal Thyroid Hormone Metabolism
Scientists found that two specific changes in a thyroid gene make the enzyme work much slower because it can't grab its fuel (thyroxine) as well — just like the claim said. They tested this directly in human cells in the lab.
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.