| Alcohol Dehydrogenase 1C (ADH1C) | |
|---|---|
| Gene | [ADH1C](/entities/adh1c) |
| UniProt ID | [P00326](https://www.uniprot.org/uniprotkb/P00326/entry) |
| PDB Structure | 1CTO, 1HLW, 2FZE |
| Molecular Weight | 39.7 kDa |
| Subcellular Localization | Cytoplasm |
| Protein Family | Alcohol dehydrogenase, zinc-containing |
ADH1C Protein is a protein. This page describes its structure, normal nervous system function, role in neurodegenerative disease, and potential as a therapeutic target.
ADH1C is a zinc-containing alcohol dehydrogenase composed of two subunits, each requiring zinc ions for structural integrity and catalytic activity[1]. The enzyme contains a catalytic zinc at the active site (Cys46, Cys174, His67) and a structural zinc bound to the tetramer interface[2]. The protein has a typical Rossmann-fold structure for NAD(P)H binding.
ADH1C is primarily known for its role in ethanol metabolism in the liver, catalyzing the oxidation of ethanol to acetaldehyde[3]. In the brain, alcohol dehydrogenase enzymes are expressed at lower levels and may play a role in retinol metabolism and dopamine catabolism[4]. ADH1C is one of the major ADH isoforms expressed in human brain tissue.
ADH1C has been implicated in Alzheimer's disease through genetic association studies. The ADH1C gene (rs698) polymorphism has been linked to increased AD risk in some populations[5]. The enzyme may affect AD pathogenesis through its role in lipid peroxidation and acetaldehyde toxicity[6].
Studies have reported associations between ADH1C variants and Parkinson's disease risk[7]. ADH1C may influence PD susceptibility through its involvement in dopamine metabolism and oxidative stress response[8].
Given its role in alcohol metabolism, ADH1C variations may influence individual susceptibility to alcohol-induced neurotoxicity and neurodegeneration[9].
ADH1C structure. UniProt. ↩︎
Zinc binding in alcohol dehydrogenases. Journal of Biological Chemistry. ↩︎
Eriksson et al. Alcohol metabolism in brain. Addiction Biology. 2001. ↩︎
Agarwal & Goedde, Alcohol dehydrogenase in brain. Pharmacology. ↩︎
Zhao et al. ADH1C and Alzheimer's disease. Neurobiology of Aging. 2006. ↩︎
ADH1C and lipid peroxidation. Free Radical Biology and Medicine. ↩︎
Sun et al. ADH1C and Parkinson's disease. Journal of Alzheimer's Disease. 2015. ↩︎
ADH1C and dopamine metabolism. Neurochemistry International. ↩︎
Alcohol and neurodegeneration. Brain Research Reviews. ↩︎
ADH1C variants and alcohol toxicity. Pharmacogenomics. ↩︎