ArticleScientific reports2018
NADH/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- In silico pathway-based subtractive proteomics for identifying novel drug targets in Candida albicans with structure-guided drug repurposing of aspartate-semialdehyde dehydrogenase inhibitors.Journal of molecular modeling · 2026Article
- A Ketol-Acid Reductoisomerase Inhibitor That Has Antituberculosis and Herbicidal Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Changes in potential pathogenicity-associated proteins ofFrontiers in microbiology · 2025Article
- Characterization of a class II ketol-acid reductoisomerase fromRSC advances · 2022Article
- Structural Rearrangements of a Dodecameric Ketol-Acid Reductoisomerase Isolated from a Marine Thermophilic Methanogen.Biomolecules · 2021Article
- Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules.Frontiers in bioinformatics · 2021Review
- The effects of vegetable pickling conditions on the dynamics of microbiota and metabolites.PeerJ · 2021Article
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7 authors.
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Abstract
Ketol-acid reductoisomerase (KARI) is a bifunctional enzyme in the second step of branched-chain amino acids biosynthetic pathway. Most KARIs prefer NADPH as a cofactor. However, KARI with a preference for NADH is desirable in industrial applications including anaerobic fermentation for the production of branched-chain amino acids or biofuels. Here, we characterize a thermoacidophilic archaeal Sac-KARI from Sulfolobus acidocaldarius and present its crystal structure at a 1.75-Å resolution. By comparison with other holo-KARI structures, one sulphate ion is observed in each binding site for the 2'-phosphate of NADPH, implicating its NADPH preference. Sac-KARI has very high affinity for NADPH and NADH, with K
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