Gnmt
D. melanogaster
Glycine N-methyltransferase
What the model saw
Gene: Gnmt Organism: Drosophila melanogaster Known functions: Glycine N-methyltransferase. glycine N-methyltransferase. S-adenosyl-L-methionine binding. glycine N-methyltransferase activity. glycine binding. identical protein binding.
View unredacted entry
Glycine N-methyltransferase. glycine N-methyltransferase. S-adenosyl-L-methionine binding. glycine N-methyltransferase activity. glycine binding. identical protein binding.
Solver output
Glycine N-methyltransferase (GNMT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to glycine, producing sarcosine and S-adenosyl-L-homocysteine (SAH). This reaction is a major regulator of the SAM:SAH ratio and one-carbon metabolism, effectively acting as a metabolic rheostat for methyl group availability. In Drosophila, Gnmt has been shown to extend lifespan by modulating SAM levels; excess SAM is associated with reduced longevity, and GNMT activity depletes SAM, thereby limiting aberrant methylation reactions. This connects directly to nutrient-sensing pathways, as SAM is a key metabolic sensor linking dietary methionine intake to downstream signaling (including mTORC1 activation). By buffering SAM levels, GNMT dampens nutrient-sensing pathway activity, mimicking the pro-longevity effects of methionine restriction.
GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.
Advisor judgment
The model correctly predicted pro_longevity for Gnmt in Drosophila melanogaster with high confidence (0.82). The mechanistic reasoning is excellent and accurate: GNMT depletes SAM, which buffers one-carbon metabolism and limits aberrant methylation, connecting to methionine restriction and mTORC1/nutrient sensing pathways. This aligns well with published literature on Gnmt in Drosophila longevity. The mechanism classification as "deregulated_nutrient_sensing" is appropriate given the SAM-mTORC1 connection.
Raw API responses
solver
{
"reasoning": "Glycine N-methyltransferase (GNMT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to glycine, producing sarcosine and S-adenosyl-L-homocysteine (SAH). This reaction is a major regulator of the SAM:SAH ratio and one-carbon metabolism, effectively acting as a metabolic rheostat for methyl group availability. In Drosophila, Gnmt has been shown to extend lifespan by modulating SAM levels; excess SAM is associated with reduced longevity, and GNMT activity depletes SAM, thereby limiting aberrant methylation reactions. This connects directly to nutrient-sensing pathways, as SAM is a key metabolic sensor linking dietary methionine intake to downstream signaling (including mTORC1 activation). By buffering SAM levels, GNMT dampens nutrient-sensing pathway activity, mimicking the pro-longevity effects of methionine restriction.",
"confidence": 0.82,
"key_pathways": [
"S-adenosylmethionine (SAM) metabolism / one-carbon metabolism",
"Methionine restriction / mTORC1 nutrient sensing",
"Methylation homeostasis"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for Gnmt in Drosophila melanogaster with high confidence (0.82). The mechanistic reasoning is excellent and accurate: GNMT depletes SAM, which buffers one-carbon metabolism and limits aberrant methylation, connecting to methionine restriction and mTORC1/nutrient sensing pathways. This aligns well with published literature on Gnmt in Drosophila longevity. The mechanism classification as \"deregulated_nutrient_sensing\" is appropriate given the SAM-mTORC1 connection.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}