Why cutting off a protein's tail makes it chew up energy faster
C-terminal Deletion of Human Tissue Transglutaminase Enhances Magnesium-dependent GTP/ATPase Activity*
Not medical advice. For informational purposes only. Always consult a healthcare professional. Terms
Scientists cut off different parts of a human protein called tTG to see how it uses energy molecules (GTP and ATP). Removing the tail made it break down energy much faster, but broke its other job.
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Researchers compare people who have a condition (cases) with similar people who do not (controls), looking back in time for differences in exposure. Useful but more prone to bias.
Not medical advice. For informational purposes only. Always consult a healthcare professional. Terms
Scientists cut off different parts of a human protein called tTG to see how it uses energy molecules (GTP and ATP). Removing the tail made it break down energy much faster, but broke its other job.
Systematic Reviews & Meta-Analyses
Max 100Randomized Controlled Trials
Max 90Cohort Studies
Max 72Case-Control Studies
Max 58Cross-Sectional Studies
Max 44Case Reports & Case Series
Max 30Expert Opinion & Narrative Reviews
Max 528 / 58
Evidence Score
Researchers compare people who have a condition (cases) with similar people who do not (controls), looking back in time for differences in exposure. Useful but more prone to bias.
Publication
Authors
Lai TS, Slaughter TF, Koropchak CM, Haroon ZA, Greenberg CS
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Claims (4)
B vitamins help enable the chemical reactions that break down sugar for energy and produce ATP, the molecule cells use for energy. Magnesium is necessary for ATP to function properly in these processes.
In human tissue transglutaminase, the rates at which the enzyme breaks down GTP and ATP change in a coordinated way when the protein is shortened at its end, indicating that both molecules are processed by the same active site.
Removing a specific segment of the human tissue transglutaminase protein decreases its ability to perform one enzymatic function by more than 95% while increasing another enzymatic function by up to 34 times, indicating that this segment normally restrains nucleotide hydrolysis.
A modified version of the human tissue transglutaminase protein, missing part of its structure, breaks down GTP 34 times faster than the normal version, while still binding to its substrate at the same rate, suggesting that the first 345 amino acids are essential for its nucleotide-breaking function.