ArticleThe Journal of biological chemistry2024
Specific residues and conformational plasticity define the substrate specificity of short-chain dehydrogenases/reductases.
Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Article
- Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia.Science advances · 2026Article
- Evolutionary engineering of Geobacillus thermoleovorans for growth on adipic acid and 1,4-butanediol.Applied microbiology and biotechnology · 2026Article
- Crystal structure of a short-chain dehydrogenase from Brucella ovis with apo and coenzyme NADActa crystallographica. Section F, Structural biology communications · 2025Article
- Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol.Angewandte Chemie (International ed. in English) · 2025Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Short-chain dehydrogenases/reductases (SDRs) are one of the most prevalent enzyme families distributed among the sequenced microorganisms. Despite the presence of a conserved catalytic tetrad and high structural similarity, these enzymes exhibit different substrate specificities. The insufficient knowledge regarding the amino acids underlying substrate specificity hinders the understanding of the SDRs' roles in diverse and significant biological processes. Here, we performed bioinformatic analysis, molecular modeling, and mutagenesis studies to identify the key residues that regulate the substrate specificities of two homologous microbial SDRs (i.e., DesE and KduD). Further, we investigated the impact of altering the physicochemical properties of these amino acids on enzyme activity. Interestingly, molecular dynamics simulations also suggest a critical role of enzyme conformational flexibility in substrate recognition and catalysis. Overall, our findings improve the understanding of microbial SDR substrate specificity and shed light on future rational design of more efficient and effective biocatalysts.
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Registered trials
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