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ADH1

S. cerevisiae

alcohol dehydrogenase ADH1

What the model saw

Gene: ADH1
Organism: Saccharomyces cerevisiae
Known functions: alcohol dehydrogenase ADH1. alcohol dehydrogenase (NAD+) activity. allyl-alcohol dehydrogenase activity. butanol dehydrogenase (NAD+) activity. ethanol dehydrogenase (NAD+) activity. identical protein binding. melatonin binding. methylglyoxal reductase (NADH) activity. octanol dehydrogenase (NAD+) activity. oxidoreductase activity. protein binding. zinc ion binding.
View unredacted entry
alcohol dehydrogenase ADH1. alcohol dehydrogenase (NAD+) activity. allyl-alcohol dehydrogenase activity. butanol dehydrogenase (NAD+) activity. ethanol dehydrogenase (NAD+) activity. identical protein binding. melatonin binding. methylglyoxal reductase (NADH) activity. octanol dehydrogenase (NAD+) activity. oxidoreductase activity. protein binding. zinc ion binding.

Solver output

Predicted influence
Anti-longevity
Confidence
72%
Mechanism
Deregulated nutrient sensing
Reasoning

ADH1 is the primary alcohol dehydrogenase in S. cerevisiae, catalyzing the conversion of acetaldehyde to ethanol during fermentative growth (NAD+/NADH-coupled). Its dominant activity drives the Crabtree effect — preferential fermentation over respiration even in the presence of oxygen — which is associated with reduced mitochondrial respiration, increased reactive oxygen species, and shortened replicative lifespan. High ADH1 activity promotes glucose-driven fermentation and suppresses the shift to respiratory metabolism that is typically associated with longevity in yeast (e.g., caloric restriction extends lifespan partly by reducing fermentative flux). Additionally, ADH1-mediated ethanol production generates acetaldehyde as a toxic intermediate and contributes to NADH/NAD+ imbalance, which can impair sirtuin (Sir2) activity that depends on NAD+ availability. The methylglyoxal reductase activity also links ADH1 to detoxification of a glycolytic byproduct, but the dominant pro-fermentation role outweighs this benefit in the context of aging.

Key pathways
fermentative glucose metabolism / Crabtree effectNAD+/NADH redox balance and sirtuin regulationethanol/acetaldehyde production and proteotoxic stress
Longevity influence
Anti-longevity
Lifespan effect
Increase

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

Answer
Correct
Mechanism
Correct
Reasoning quality
4/5
Failure mode
Correct
Notes

The model correctly predicted ADH1 as anti_longevity in S. cerevisiae with reasonable confidence (0.72). The mechanistic reasoning is largely sound: ADH1 promotes fermentative metabolism (Crabtree effect), which is associated with shortened lifespan; the connection to NAD+/NADH balance and sirtuin regulation is well-established in yeast aging literature. The model correctly notes that deletion of ADH1 would shift metabolism toward respiration, which is associated with extended lifespan. The reasoning about acetaldehyde toxicity and methylglyoxal reductase activity adds nuance. One minor issue: the model classifies the mechanism as "deregulated_nutrient_sensing" which is a somewhat imprecise label for what is primarily a metabolic/redox mechanism, but the textual reasoning itself is accurate. Overall a strong, well-reasoned prediction.

Raw API responses

solver

{
  "reasoning": "ADH1 is the primary alcohol dehydrogenase in S. cerevisiae, catalyzing the conversion of acetaldehyde to ethanol during fermentative growth (NAD+/NADH-coupled). Its dominant activity drives the Crabtree effect — preferential fermentation over respiration even in the presence of oxygen — which is associated with reduced mitochondrial respiration, increased reactive oxygen species, and shortened replicative lifespan. High ADH1 activity promotes glucose-driven fermentation and suppresses the shift to respiratory metabolism that is typically associated with longevity in yeast (e.g., caloric restriction extends lifespan partly by reducing fermentative flux). Additionally, ADH1-mediated ethanol production generates acetaldehyde as a toxic intermediate and contributes to NADH/NAD+ imbalance, which can impair sirtuin (Sir2) activity that depends on NAD+ availability. The methylglyoxal reductase activity also links ADH1 to detoxification of a glycolytic byproduct, but the dominant pro-fermentation role outweighs this benefit in the context of aging.",
  "confidence": 0.72,
  "key_pathways": [
    "fermentative glucose metabolism / Crabtree effect",
    "NAD+/NADH redox balance and sirtuin regulation",
    "ethanol/acetaldehyde production and proteotoxic stress"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "anti_longevity"
}

advisor

{
  "notes": "The model correctly predicted ADH1 as anti_longevity in S. cerevisiae with reasonable confidence (0.72). The mechanistic reasoning is largely sound: ADH1 promotes fermentative metabolism (Crabtree effect), which is associated with shortened lifespan; the connection to NAD+/NADH balance and sirtuin regulation is well-established in yeast aging literature. The model correctly notes that deletion of ADH1 would shift metabolism toward respiration, which is associated with extended lifespan. The reasoning about acetaldehyde toxicity and methylglyoxal reductase activity adds nuance. One minor issue: the model classifies the mechanism as \"deregulated_nutrient_sensing\" which is a somewhat imprecise label for what is primarily a metabolic/redox mechanism, but the textual reasoning itself is accurate. Overall a strong, well-reasoned prediction.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 4,
  "ground_truth_questionable": false
}