ArticleScientific reports2015
Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 16 citations in OpenAlex.
- Highly efficient biosynthesis of spermidine from L-homoserine and putrescine using an engineered Escherichia coli with NADPH self-sufficient system.Applied microbiology and biotechnology · 2022Article
- Conformational changes in the catalytic region are responsible for heat-induced activation of hyperthermophilic homoserine dehydrogenase.Communications biology · 2022Article
- Molecular and Enzymatic Features of Homoserine Dehydrogenase fromJournal of microbiology and biotechnology · 2020Article
- Crystal structure of the NADPExtremophiles : life under extreme conditions · 2018Article
- Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex.Scientific reports · 2018Article
- Molecular Mechanisms of Enzyme Activation by Monovalent Cations.The Journal of biological chemistry · 2016Review
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
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Abstract
NAD(P)-dependent dehydrogenases differ according to their coenzyme preference: some prefer NAD, others NADP, and still others exhibit dual cofactor specificity. The structure of a newly identified archaeal homoserine dehydrogenase showed this enzyme to have a strong preference for NADP. However, NADP did not act as a cofactor with this enzyme, but as a strong inhibitor of NAD-dependent homoserine oxidation. Structural analysis and site-directed mutagenesis showed that the large number of interactions between the cofactor and the enzyme are responsible for the lack of reactivity of the enzyme towards NADP. This observation suggests this enzyme exhibits a new variation on cofactor binding to a dehydrogenase: very strong NADP binding that acts as an obstacle to NAD(P)-dependent dehydrogenase catalytic activity.
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