ArticleThe Biochemical journal2015
Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Potassium binding by carbonyl clusters, halophilic adaptation and catalysis of Haloferax mediterranei D-2-hydroxyacid dehydrogenase.Communications biology · 2025Article
- A Ketol-Acid Reductoisomerase Inhibitor That Has Antituberculosis and Herbicidal Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Structural Rearrangements of a Dodecameric Ketol-Acid Reductoisomerase Isolated from a Marine Thermophilic Methanogen.Biomolecules · 2021Article
- NADH/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius.Scientific reports · 2018Article
- Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.Biochemistry · 2017Review
- A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.ACS synthetic biology · 2017Article
- Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases.Protein science : a publication of the Protein Society · 2016Article
- Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.Protein engineering, design & selection : PEDS · 2016Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Although most sequenced members of the industrially important ketol-acid reductoisomerase (KARI) family are class I enzymes, structural studies to date have focused primarily on the class II KARIs, which arose through domain duplication. In the present study, we present five new crystal structures of class I KARIs. These include the first structure of a KARI with a six-residue β2αB (cofactor specificity determining) loop and an NADPH phosphate-binding geometry distinct from that of the seven- and 12-residue loops. We also present the first structures of naturally occurring KARIs that utilize NADH as cofactor. These results show insertions in the specificity loops that confounded previous attempts to classify them according to loop length. Lastly, we explore the conformational changes that occur in class I KARIs upon binding of cofactor and metal ions. The class I KARI structures indicate that the active sites close upon binding NAD(P)H, similar to what is observed in the class II KARIs of rice and spinach and different from the opening of the active site observed in the class II KARI of Escherichia coli. This conformational change involves a decrease in the bending of the helix that runs between the domains and a rearrangement of the nicotinamide-binding site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.