GO:0004022 alcohol dehydrogenase (NAD+) activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004022 alcohol dehydrogenase (NAD+) activity describes the catalysis of an alcohol + NAD+ to an aldehyde or ketone + NADH + H+.
• The term covers NAD-dependent oxidation of primary, secondary, aliphatic and aromatic alcohols, and is synonymous with ADH, ethanol dehydrogenase and aldehyde dehydrogenase (NAD) activity.
• Enzymes with this activity are central to ethanol metabolism, alkane degradation, methylglyoxal detoxification and redox homeostasis [1,2,7].
• Altered alcohol dehydrogenase (NAD+) activity has been linked to hepatic fibrogenesis, hepatocellular carcinoma prognosis and gastric ethanol metabolism [4,5,6].
• Microbial and archaeal ADHs, such as HwADH from Haloquadratum walsbyi, show dual NAD+/NADP+ affinity and thermostability, making them attractive biocatalysts.
• CRISPR knockout, point-mutation, knock-in and overexpression models enable causal dissection of ADH-encoding genes in disease and metabolism [5,6].
Description
GO:0004022 alcohol dehydrogenase (NAD+) activity is a molecular function defined as the catalysis of the reaction: an alcohol + NAD+ = an aldehyde or ketone + NADH + H+. This activity is widely distributed across prokaryotes, fungi, plants and animals, and it underpins the first step in ethanol oxidation, the interconversion of alcohols and carbonyl compounds, and the maintenance of cellular redox balance [1,2,7]. Because NAD+ is the electron acceptor, the reaction directly couples alcohol oxidation to the NADH/NAD+ ratio, a central node in energy metabolism and oxidative stress responses [2,7]. Researchers study alcohol dehydrogenase (NAD+) activity to understand how organisms detoxify alcohols, how pathogens such as Helicobacter pylori and Candida albicans handle reactive aldehydes, and how human tissues metabolize ethanol [2,3,7]. In humans, gastric and hepatic ADH activity influences blood ethanol levels and has been associated with fibrogenesis and cancer prognosis [4,5,6]. In biotechnology, thermostable and dual-affinity ADHs are pursued for chiral alcohol synthesis and cofactor recycling. The term is therefore a convergence point for enzymology, infectious disease, cancer biology and metabolic engineering. This article summarizes the QuickGO definition, the genes and proteins that carry this activity, the mechanistic steps, disease links, and the CRISPR-based methods used to interrogate it.
alcohol dehydrogenase (NAD+) activity At A Glance
| GO ID | GO:0004022 |
|---|---|
| GO term | alcohol dehydrogenase (NAD+) activity |
| Ontology | molecular_function |
| Synonym | ADH; alcohol dehydrogenase activity; alcohol:NAD+ oxidoreductase; aldehyde dehydrogenase (NAD) activity; aldo-keto reductase (NAD) activity; aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase |
| Definition | Catalysis of the reaction: an alcohol + NAD+ = an aldehyde or ketone + NADH + H+. |
| Major function | NAD+-dependent oxidation of alcohols to aldehydes or ketones, coupled to NADH production. |
| Cofactor | NAD+ (nicotinamide adenine dinucleotide, oxidized form) |
| Substrate scope | Primary, secondary, aliphatic and aromatic alcohols; ethanol is a common substrate. |
| Reaction direction | Reversible; oxidation of alcohol or reduction of aldehyde/ketone depending on NADH/NAD+ ratio. |
What Is GO:0004022?
GO:0004022 alcohol dehydrogenase (NAD+) activity is the catalytic function of an enzyme that transfers a hydride from an alcohol substrate to NAD+, producing the corresponding aldehyde or ketone, NADH and a proton. The reaction is reversible and can also reduce aldehydes or ketones back to alcohols when NADH is abundant [1,7]. The term is specific to NAD+ as the preferred cofactor, distinguishing it from NADP+-dependent alcohol dehydrogenases, although some enzymes such as HwADH exhibit dual NAD+/NADP+ affinity. Synonyms include ADH, alcohol dehydrogenase activity, alcohol:NAD+ oxidoreductase, aldehyde dehydrogenase (NAD) activity, aldo-keto reductase (NAD) activity, aliphatic alcohol dehydrogenase, ethanol dehydrogenase, NAD-dependent alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, NAD-specific aromatic alcohol dehydrogenase, primary alcohol dehydrogenase and yeast alcohol dehydrogenase.
Why Is alcohol dehydrogenase (NAD+) activity Important in Cell Biology?
Alcohol dehydrogenase (NAD+) activity is important because it controls the first committed step of ethanol metabolism, determines the cellular balance between alcohols and reactive aldehydes, and regenerates NADH for biosynthetic and bioenergetic pathways [1,2,7]. In humans, gastric ADH modulates blood ethanol levels after drinking, and hepatic ADH activity correlates with fibrogenesis and influences hepatocellular carcinoma prognosis [4,5,6]. In pathogens, ADH-dependent methylglyoxal detoxification supports survival and virulence, as shown in Candida albicans [2,7]. In environmental and industrial microbiology, ADHs enable long-chain alkane degradation and provide thermostable biocatalysts for chiral alcohol production [1,8]. Consequently, this GO term is a focal point for studies of addiction, liver disease, cancer, infectious disease and green chemistry.
• Catalyzes the first step of ethanol oxidation, controlling blood ethanol clearance and acetaldehyde exposure [3,4].
• Regulates methylglyoxal concentration and glutathione-dependent enzyme activities in Candida albicans [2,7].
• Correlates with hepatic fibrogenesis and may serve as a marker of liver injury.
• Influences prognosis of hepatocellular carcinoma patients together with acetaldehyde dehydrogenases.
• Supports long-chain alkane degradation in Acinetobacter venetianus RAG-1.
• Provides thermostable, dual-affinity biocatalysts such as HwADH for industrial applications.
• Links alcohol metabolism to NADH/NAD+ redox balance and oxidative stress responses [2,7].
• Is a target for pharmacological modulation, e.g., cimetidine effects on gastric ADH and blood ethanol.
• Enables comparative enzymology across bacteria, fungi, archaea and humans [1,2,8].
• Underpins CRISPR-based functional studies of ADH-encoding genes in disease models [5,6].
Molecular Mechanism of alcohol dehydrogenase (NAD+) activity
Substrate binding and cofactor selection
In simple terms: The enzyme first grabs the alcohol and the NAD+ cofactor.
Alcohol dehydrogenase (NAD+) enzymes bind an alcohol substrate and the oxidized cofactor NAD+ in a ordered or random sequential mechanism. The active site typically contains a catalytic zinc ion that polarizes the alcohol hydroxyl group, facilitating hydride transfer [1,8]. Some enzymes, such as HwADH from Haloquadratum walsbyi, can also use NADP+, giving dual cofactor affinity. Substrate specificity ranges from short-chain ethanol to long-chain alkanes and aromatic alcohols, depending on the enzyme family [1,3].
Hydride transfer and product release
In simple terms: A hydride is moved from the alcohol to NAD+, making an aldehyde and NADH.
The catalytic step involves stereospecific transfer of a hydride from the alcohol carbon to the nicotinamide ring of NAD+, yielding an aldehyde or ketone, NADH and a proton. The reaction is reversible, so the same enzyme can reduce aldehydes or ketones when NADH is abundant [1,7]. Product release regenerates the free enzyme for subsequent cycles, and the overall rate depends on substrate and cofactor concentrations [1,2].
Role in methylglyoxal detoxification
In simple terms: ADH helps remove a toxic byproduct called methylglyoxal.
In Candida albicans, NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration, and ADH1 together with NAD(H)-linked methylglyoxal oxidoreductase reciprocally controls glutathione-dependent enzyme activities [2,7]. This detoxification function links alcohol dehydrogenase (NAD+) activity to redox homeostasis and virulence in fungal pathogens [2,7].
Alkane degradation and environmental adaptation
In simple terms: Some bacteria use ADH to break down long-chain alkanes.
An NAD+-dependent group III alcohol dehydrogenase is involved in long-chain alkane degradation in Acinetobacter venetianus RAG-1. This activity allows the bacterium to oxidize alkanes to corresponding alcohols and aldehydes, feeding them into central metabolism. Such enzymes expand the ecological and biotechnological relevance of GO:0004022 beyond ethanol metabolism.
Regulation by cofactor ratio and gene expression
In simple terms: The enzyme's direction and speed depend on NADH/NAD+ levels and how much enzyme is made.
Because the reaction is reversible, the NADH/NAD+ ratio dictates whether alcohol oxidation or aldehyde reduction predominates [1,7]. Expression of ADH-encoding genes is also regulated in response to substrate availability and stress, as seen in Candida albicans and Acinetobacter venetianus [1,2]. Pharmacological agents such as cimetidine can inhibit gastric ADH activity and alter blood ethanol levels, demonstrating post-translational and tissue-specific regulation.
Key Genes Involved in GO:0004022 alcohol dehydrogenase (NAD+) activity
The following genes and proteins carry or are directly associated with alcohol dehydrogenase (NAD+) activity across microbial, archaeal and human systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ADH1 (Candida albicans) | NAD+-linked alcohol dehydrogenase 1; regulates methylglyoxal concentration | Fungal virulence and redox homeostasis [2,7] |
| ADH1 (Homo sapiens) | Class I alcohol dehydrogenase; oxidizes ethanol to acetaldehyde | Ethanol metabolism, liver disease, cancer prognosis [5,6] |
| ADH2 (Homo sapiens) | Class I alcohol dehydrogenase; contributes to hepatic ethanol oxidation | Genetic polymorphisms and alcohol-related disease |
| ADH3 (Homo sapiens) | Class I alcohol dehydrogenase; involved in formaldehyde and alcohol metabolism | Tissue-specific ethanol clearance |
| ADH4 (Homo sapiens) | Class II alcohol dehydrogenase; oxidizes longer-chain alcohols | Substrate specificity studies |
| ADH5 (Homo sapiens) | Class III alcohol dehydrogenase; formaldehyde dehydrogenase activity | Formaldehyde detoxification and redox balance |
| ADH6 (Homo sapiens) | Class V alcohol dehydrogenase; broad substrate range | Xenobiotic and alcohol metabolism |
| ADH7 (Homo sapiens) | Class IV alcohol dehydrogenase; gastric and mucosal ethanol oxidation | First-pass ethanol metabolism [3,4] |
| HwADH (Haloquadratum walsbyi) | Thermostable, NAD+/NADP+ dual-affinity alcohol dehydrogenase | Industrial biocatalysis |
| Group III ADH (Acinetobacter venetianus RAG-1) | NAD+-dependent alcohol dehydrogenase for long-chain alkane degradation | Bioremediation and alkane metabolism |
| MGO (Candida albicans) | NAD(H)-linked methylglyoxal oxidoreductase; interacts with ADH1 | Methylglyoxal detoxification |
| Helicobacter pylori ADH | Alcohol dehydrogenase activity in gastric pathogen | Gastric ethanol metabolism and infection |
| ALDH2 (Homo sapiens) | Acetaldehyde dehydrogenase; downstream of ADH | Alcohol-related cancer risk |
| Gastric ADH (Homo sapiens) | Gastric mucosa alcohol dehydrogenase | First-pass ethanol metabolism and drug interactions |
| Hepatic ADH (Homo sapiens) | Liver alcohol dehydrogenase activity | Hepatic fibrogenesis and liver injury |
| Yeast ADH (Saccharomyces cerevisiae) | Classic NAD+-dependent alcohol dehydrogenase | Model enzymology and fermentation |
| Aromatic ADH (various) | NAD-specific aromatic alcohol dehydrogenase | Biotransformation of aromatic alcohols |
How Is alcohol dehydrogenase (NAD+) activity Regulated?
Alcohol dehydrogenase (NAD+) activity is regulated at multiple levels. The reaction direction and rate depend on the NADH/NAD+ ratio, because the enzyme catalyzes a reversible redox interconversion [1,7]. In Candida albicans, ADH1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities, linking ADH function to oxidative stress responses. Expression of ADH-encoding genes responds to substrate availability and environmental conditions, as observed in Acinetobacter venetianus RAG-1 during alkane degradation. Pharmacological inhibition by cimetidine reduces gastric ADH activity and raises blood ethanol levels, showing that the activity can be modulated in vivo. Genetic polymorphisms in ADH genes further influence enzyme content and metabolic activity in humans.
alcohol dehydrogenase (NAD+) activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ADH1 (Homo sapiens) | Hepatic fibrogenesis; alcohol-related liver injury | CRISPR knockout hepatocyte cell line; overexpression in hepatic stellate cells |
| ADH1/ADH2 (Homo sapiens) | Hepatocellular carcinoma prognosis | Point-mutation knock-in of polymorphisms in liver cancer cells |
| ADH7 (Homo sapiens) | Gastric ethanol metabolism; drug-alcohol interaction | Gastric epithelial knockout and cimetidine treatment |
| ADH1 (Candida albicans) | Fungal virulence; methylglyoxal detoxification | CRISPR knockout in C. albicans; methylglyoxal sensitivity assay [2,7] |
| Helicobacter pylori ADH | Gastric infection and ethanol metabolism | Bacterial ADH knockout and gastric cell co-culture |
Alcohol dehydrogenase (NAD+) activity in liver disease and fibrogenesis
Higher activity of alcohol dehydrogenase is correlated with hepatic fibrogenesis, suggesting that ADH-mediated ethanol oxidation and acetaldehyde production contribute to liver injury and fibrosis. Gastric ADH also participates in first-pass ethanol metabolism, and its inhibition by cimetidine increases blood ethanol levels, which is relevant to drug-alcohol interactions. These findings position ADH activity as a modifier of alcohol-related liver pathology [4,5].
Alcohol dehydrogenase (NAD+) activity and hepatocellular carcinoma prognosis
Gene polymorphisms, metabolic activity and content of alcohol dehydrogenase and acetaldehyde dehydrogenases affect the prognosis of hepatocellular carcinoma patients. This indicates that ADH-driven acetaldehyde exposure and redox changes may influence tumor progression and treatment outcomes. The same study highlights the importance of combined ADH/ALDH genotyping in cancer risk stratification.
Alcohol dehydrogenase (NAD+) activity in gastric infection and ethanol metabolism
Helicobacter pylori possesses alcohol dehydrogenase activity, and gastric ADH contributes to ethanol metabolism in the stomach [3,4]. Infection and pharmacological agents can alter gastric ADH activity, thereby changing blood ethanol concentrations [3,4]. This links GO:0004022 to infectious disease and to the pharmacokinetics of alcohol [3,4].
Alcohol dehydrogenase (NAD+) activity in fungal virulence and methylglyoxal detoxification
In Candida albicans, NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration and, together with methylglyoxal oxidoreductase, reciprocally controls glutathione-dependent enzyme activities [2,7]. Loss of this regulation impairs detoxification of reactive carbonyl species, which are cytotoxic and contribute to fungal virulence [2,7]. Thus, ADH activity is a potential antifungal target [2,7].
From alcohol dehydrogenase (NAD+) activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of ADH1 reduce ethanol oxidation? | CRISPR knockout of ADH1 in hepatocyte cell lines |
| Does a specific ADH polymorphism alter enzyme activity? | Point-mutation knock-in of the variant in a cell line |
| Can ADH1 be tagged for localization studies? | Tagged knock-in of ADH1 with fluorescent or affinity tag |
| Does ADH1 overexpression increase methylglyoxal detoxification? | Overexpression of ADH1 in Candida albicans |
| Does ADH activity affect gastric ethanol metabolism? | Gastric epithelial knockout plus cimetidine treatment |
| Can thermostable ADH be engineered for biocatalysis? | Overexpression of HwADH in a heterologous host |
How to Study the alcohol dehydrogenase (NAD+) activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| NADH absorbance assay | Alcohol dehydrogenase (NAD+) activity | Kinetic characterization of ADH enzymes [1,8] |
| qPCR / RNA-seq | ADH gene expression | Expression profiling in pathogens and human tissues [1,2] |
| Genotyping | ADH polymorphisms | Cancer prognosis and risk stratification |
| CRISPR knockout | Loss-of-function phenotype | Causal testing of ADH genes in disease models |
| CRISPR knock-in | Variant-specific effects | Polymorphism functional studies |
| Tagged knock-in | Protein localization and interactions | Subcellular localization of ADH |
| Methylglyoxal assay | Reactive carbonyl detoxification | Fungal virulence studies |
| Blood ethanol measurement | In vivo ethanol clearance | Drug-alcohol interaction studies |
Enzymatic activity assays
Alcohol dehydrogenase (NAD+) activity is typically measured spectrophotometrically by monitoring NADH formation at 340 nm using ethanol or other alcohols as substrates [1,8]. These assays can determine kinetic parameters, cofactor preference and thermostability, as shown for HwADH. They are also used to compare activity in tissue homogenates, such as gastric or hepatic samples [4,5].
Gene expression and polymorphism analysis
Quantitative PCR, RNA-seq and genotyping are used to measure ADH gene expression and to identify polymorphisms that affect enzyme content and metabolic activity. Such analyses have linked ADH and ALDH genotypes to hepatocellular carcinoma prognosis. Expression profiling in Candida albicans and Acinetobacter venetianus has also revealed regulation of ADH genes under stress or alkane exposure [1,2].
CRISPR-based functional genomics
CRISPR knockout, point-mutation knock-in and overexpression models allow causal testing of ADH-encoding genes [5,6]. For example, knocking out ADH1 in hepatocytes can reveal its contribution to fibrogenesis, while knock-in of polymorphisms can test their effect on enzyme activity [5,6]. Tagged knock-in enables localization and interaction studies.
Metabolite and redox measurements
Measuring methylglyoxal, glutathione-dependent enzyme activities and NADH/NAD+ ratios provides functional readouts of ADH activity [2,7]. These methods are especially useful in Candida albicans, where ADH1 regulates methylglyoxal concentration. In human samples, blood ethanol levels after cimetidine treatment reflect gastric ADH activity.
How CRISPR Can Be Used to Study GO:0004022 alcohol dehydrogenase (NAD+) activity
Knockout
CRISPR knockout of ADH-encoding genes is used to eliminate alcohol dehydrogenase (NAD+) activity and assess downstream phenotypes such as reduced ethanol oxidation, altered methylglyoxal levels or impaired fibrogenesis [5,7]. Knockout models provide causal evidence that a specific gene carries the activity in a given cell type.
Point Mutation
Point-mutation knock-in introduces specific polymorphisms into ADH genes to test their effect on enzyme activity, substrate specificity or disease prognosis. This approach is valuable for dissecting the contribution of individual variants identified in human genetic studies.
Knock-in
Knock-in of tags or reporter sequences allows visualization and immunoprecipitation of ADH proteins, enabling localization and interaction studies. Knock-in can also be used to replace the endogenous promoter with a regulatable element for controlled expression.
Overexpression
Overexpression of ADH genes, such as ADH1 in Candida albicans or HwADH in a heterologous host, is used to increase enzyme activity and study its effects on methylglyoxal detoxification or biocatalysis [7,8]. Overexpression models help establish sufficiency of the activity for a given phenotype [7,8].
How EDITGENE Supports alcohol dehydrogenase (NAD+) activity Research
Researchers studying alcohol dehydrogenase (NAD+) activity-related genes often need to determine whether a candidate gene is causally involved in a metabolic or disease phenotype, and CRISPR-based models provide the most direct way to test this. EDITGENE offers a suite of services to generate such models efficiently.
Contact EDITGENE today to design your custom CRISPR model for alcohol dehydrogenase (NAD+) activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ADH4 Knockout HEK293 Cell Line | EDJ-KQ2163 | Human | 127 | Details Get a Quote |
| ADH1B Knockout HEK293 Cell Line | EDJ-KQ2706 | Human | 125 | Details Get a Quote |
| ADH6 Knockout HEK293 Cell Line | EDJ-KQ3359 | Human | 130 | Details Get a Quote |
| ADH7 Knockout HEK293 Cell Line | EDJ-KQ3532 | Human | 131 | Details Get a Quote |
| ADH1A Knockout HEK293 Cell Line | EDJ-KQ3734 | Human | 124 | Details Get a Quote |
| ADH5 Knockout HEK293 Cell Line | EDJ-KQ4010 | Human | 128 | Details Get a Quote |
| ADH1C Knockout HEK293 Cell Line | EDJ-KQ4011 | Human | 126 | Details Get a Quote |
| SORD Knockout HEK293 Cell Line | EDJ-KQ5821 | Human | 6652 | Details Get a Quote |
| DHRS9 Knockout HEK293 Cell Line | EDJ-KQ6930 | Human | 10170 | Details Get a Quote |
| ADHFE1 Knockout HEK293 Cell Line | EDJ-KQ9397 | Human | 137872 | Details Get a Quote |
| ADH5 Knockout A-549 Cell Line | EDJ-KQ24993 | Human | 128 | Details Get a Quote |
| ADHFE1 Knockout HCT 116 Cell Line | EDJ-KQ36045 | Human | 137872 | Details Get a Quote |
| ADH5 Knockout HeLa Cell Line | EDJ-KQ26336 | Human | 128 | Details Get a Quote |
| SORD Knockout A-549 Cell Line | EDJ-KQ29253 | Human | 6652 | Details Get a Quote |
| SORD Knockout HCT 116 Cell Line | EDJ-KQ29254 | Human | 6652 | Details Get a Quote |
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Frequently Asked Questions About alcohol dehydrogenase (NAD+) activity
What is alcohol dehydrogenase (NAD+) activity?
It is the catalytic function defined by GO:0004022, where an enzyme converts an alcohol and NAD+ into an aldehyde or ketone, NADH and H+.
What genes are involved in alcohol dehydrogenase (NAD+) activity?
Genes include human ADH1, ADH2, ADH3, ADH4, ADH5, ADH6 and ADH7, Candida albicans ADH1, Haloquadratum walsbyi HwADH and bacterial group III ADH [1,2,6,8].
What is the reaction catalyzed by alcohol dehydrogenase (NAD+)?
The reaction is: an alcohol + NAD+ = an aldehyde or ketone + NADH + H+.
How is alcohol dehydrogenase (NAD+) activity measured?
It is commonly measured by monitoring NADH formation at 340 nm in the presence of an alcohol substrate and NAD+ [1,8].
What diseases are linked to alcohol dehydrogenase (NAD+) activity?
It has been linked to hepatic fibrogenesis, hepatocellular carcinoma prognosis, gastric ethanol metabolism and fungal virulence [2,4,5,6,7].
What is the difference between ADH and ALDH?
ADH oxidizes alcohols to aldehydes using NAD+, while ALDH oxidizes aldehydes to acids; both act sequentially in ethanol metabolism.
Can CRISPR be used to study alcohol dehydrogenase (NAD+) activity?
Yes, CRISPR knockout, point-mutation knock-in, knock-in and overexpression models are used to test the causal role of ADH genes [5,6].
What is the role of ADH1 in Candida albicans?
ADH1 regulates methylglyoxal concentration and reciprocally controls glutathione-dependent enzyme activities with methylglyoxal oxidoreductase [2,7].
Is alcohol dehydrogenase (NAD+) activity reversible?
Yes, the reaction is reversible; the direction depends on the NADH/NAD+ ratio and substrate concentrations [1,7].
What cofactor does alcohol dehydrogenase (NAD+) use?
It uses NAD+ as the preferred electron acceptor, although some enzymes such as HwADH can also use NADP+ [1,8].
Conclusion
GO:0004022 alcohol dehydrogenase (NAD+) activity is a fundamental molecular function that couples alcohol oxidation to NADH production and influences ethanol metabolism, redox homeostasis, microbial virulence and cancer biology [1,2,5,6,7]. Its broad substrate range and reversibility make it relevant to biotechnology and environmental microbiology as well [1,8]. CRISPR-based knockout, point-mutation, knock-in and overexpression models provide the tools needed to dissect the causal roles of ADH-encoding genes in these contexts [5,6]. Continued research on this activity will clarify its contributions to human disease and its potential as a therapeutic or biocatalytic target [4,5,6,8].
References
- 1. Chen S et al.. 2024. An NAD(+)-dependent group Ⅲ alcohol dehydrogenase involved in long-chain alkane degradation in Acinetobacter venetianus RAG-1.. Enzyme Microb Technol 172:110343 PMID: 37890395
- 2. Kang SO et al.. 2021. Alcohol dehydrogenase 1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities in Candida albicans.. J Microbiol 59(1):76-91 PMID: 33355888
- 3. Salaspuro M. 1994. Helicobacter pylori alcohol dehydrogenase.. EXS 71:185-95 PMID: 8032149
- 4. Caballeria J et al.. 1989. Effects of cimetidine on gastric alcohol dehydrogenase activity and blood ethanol levels.. Gastroenterology 96(2 Pt 1):388-92 PMID: 2910758
- 5. Gao N et al.. 2018. Higher Activity of Alcohol Dehydrogenase Is Correlated with Hepatic Fibrogenesis.. J Pharmacol Exp Ther 367(3):473-482 PMID: 30228113
- 6. Gao N et al.. 2022. Effects of Gene Polymorphisms, Metabolic Activity, and Content of Alcohol Dehydrogenase and Acetaldehyde Dehydrogenases on Prognosis of Hepatocellular Carcinoma Patients.. Turk J Gastroenterol 33(7):606-614 PMID: 35879918
- 7. Kwak MK et al.. 2014. NAD(+)-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans.. FEBS Lett 588(7):1144-53 PMID: 24607541
- 8. Cassidy J et al.. 2018. Haloquadratum walsbyi Yields a Versatile, NAD(+)/NADP(+) Dual Affinity, Thermostable, Alcohol Dehydrogenase (HwADH).. Mol Biotechnol 60(6):420-426 PMID: 29654471
