Alcohol Dehydrogenase Characterization in Microbial Systems
Summary
Alcohol dehydrogenases (ADHs) are a diverse group of enzymes that catalyse the reversible oxidation of alcohols to their corresponding aldehydes or ketones, playing central roles in microbial metabolism, stress resistance and biotechnological applications. In bacteria and archaea, ADHs contribute to fermentative pathways that underpin biofuel production, while in pathogenic species they can modulate virulence through detoxification of host‐derived compounds. Structurally, microbial ADHs fall into distinct families, notably zinc-dependent (typical medium‐chain) ADHs, iron-containing ADHs (FeADHs) and short-chain dehydrogenases/reductases, each defined by characteristic metal-binding motifs and cofactor specificities. Recent efforts have focused on elucidating the sequence–structure–function relationships that govern substrate specificity, catalytic efficiency and thermostability, with an eye to engineering robust biocatalysts for industrial processes. Advances in recombinant expression, high-resolution structural biology and site-directed mutagenesis have revealed how metal coordination and domain architecture contribute to enzyme dynamics under extreme conditions and in the presence of novel substrates. This expanding knowledge not only deepens our understanding of microbial physiology but also informs the rational design of ADHs for sustainable chemical synthesis, detoxification of environmental pollutants and improved microbial cell factories.
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Alcohol Dehydrogenase Characterization in Microbial Systems publication trend
The graph below shows the total number of articles in alcohol dehydrogenase characterization in microbial systems across all publications each year (not limited to Nature Index journals).
Technical terms
Alcohol dehydrogenase (ADH): An enzyme that catalyses the reversible oxidation of alcohols to aldehydes or ketones, often using NAD(P)+ as cofactor.
Iron-containing ADH (FeADH): A subclass of ADHs that coordinate one or more Fe2+ ions in their active site, contributing to catalysis and structural stability.
Rossmann fold: A common α/β structural motif that binds dinucleotide cofactors such as NAD+ or NADP+.
Thermostability: The ability of an enzyme to retain structural integrity and catalytic activity at elevated temperatures.
Oligomerisation: Assembly of individual enzyme subunits into multimeric complexes, often essential for full activity and stability.
References
- Molecular Characterization of the Iron-Containing Alcohol Dehydrogenase from the Extremely Thermophilic Bacterium Pseudothermotoga hypogea. Microorganisms (2024).
- Structural and Biochemical Analysis of the Furan Aldehyde Reductase YugJ from Bacillus subtilis. International Journal of Molecular Sciences (2022).
- Role of Iron-Containing Alcohol Dehydrogenases in Acinetobacter baumannii ATCC 19606 Stress Resistance and Virulence. International Journal of Molecular Sciences (2021).
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