Industrial light at the end of the iron‐containing (group III) alcohol dehydrogenase tunnel

Abstract

There are three prominent alcohol dehydrogenases superfamilies: short‐chain, medium‐chain, and iron‐containing alcohol dehydrogenases (FeADHs). Many members are valuable catalysts for producing industrially relevant products such as active pharmaceutical intermediates, chiral synthons, biopolymers, biofuels, and secondary metabolites. However, FeADHs are the least explored enzymes among the superfamilies for commercial tenacities. They portray a conserved structure having a “tunnel‐like” cofactor and substrate binding site with particular functions, despite representing high sequence diversity. Interestingly, phylogenetic analysis demarcates enzymes catalyzing distinct native substrates where closely related clades convert similar molecules. Further, homologs from various mesophilic and thermophilic microbes have been explored for designing a solvent and temperature‐resistant enzyme for industrial purposes. The review explores different iron‐containing alcohol dehydrogenases potential engineering of the enzymes and substrates helpful in manufacturing commercial products.

Molecular Characterization of the Iron-Containing Alcohol Dehydrogenase from the Extremely Thermophilic Bacterium Pseudothermotoga hypogea

“…They are ubiquitous in all three domains of life and are classified into three groups based on their sizes: short-chain (group I), medium-chain (group II), and long-chain (group III) ADHs, respectively. Based on the metal content, ADHs can be classified into the following categories: metal-free ADHs, zinc-containing ADHs, and Fe-dependent ADHs, which correspond to group I, II, and III ADHs, respectively [ 3 , 4 ]. Zinc ions have catalytic or structural functions in several enzymes including hyperthermophilic zinc-containing ADHs; however, only a limited number of iron-dependent ADHs are characterized, owing to their instability [ 5 ].…”

Reducing the vicissitudes of heterologous prochiral substrate catalysis by alcohol dehydrogenases through machine learning algorithms

“…Further, Type III enzymes are known to catalyze aliphatic primary and secondary alcohols. Therefore, for the production of chiral synthons production that predominantly consists aromatic rings it isn't useful [17]. On the other hand many MDRs or Type I alcohol dehydrogenases are reported to produce chiral alcohols.…”