ArticleScientific reports2015
Novel type II and monomeric NAD+ specific isocitrate dehydrogenases: phylogenetic affinity, enzymatic characterization, and evolutionary implication.
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 18 papers.
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18 citing papers in PubMed, 34 citations in OpenAlex.
- Functional redundancy driven by isocitrate dehydrogenase enhances metabolic robustness in Pseudomonas putida KT2440.Microbial cell factories · 2026Article
- Molecular insights and functional analysis of isocitrate dehydrogenase in two gram-negative pathogenic bacteria.World journal of microbiology & biotechnology · 2024Article
- Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids.Genome biology and evolution · 2024Article
- Two Different Isocitrate Dehydrogenases fromInternational journal of molecular sciences · 2023Article
- Enzymatic Characterization of the Isocitrate Dehydrogenase with Dual Coenzyme Specificity from the Marine BacteriumInternational journal of molecular sciences · 2023Article
- From a dimer to a monomer: Construction of a chimeric monomeric isocitrate dehydrogenase.Protein science : a publication of the Protein Society · 2021Article
- Evolution of a key enzyme of aerobic metabolism reveals Proterozoic functional subunit duplication events and an ancient origin of animals.Scientific reports · 2021Article
- Biochemical and Phylogenetic Characterization of a Novel NADPFrontiers in molecular biosciences · 2021Article
- Biochemical Characterization and Crystal Structure of a Novel NADInternational journal of molecular sciences · 2020Article
- Determining the interaction status and evolutionary fate of duplicated homomeric proteins.PLoS computational biology · 2020Article
- Evolution of new enzymes by gene duplication and divergence.The FEBS journal · 2020Review
- Biochemical and phylogenetic characterization of a monomeric isocitrate dehydrogenase from a marine methanogenic archaeon Methanococcoides methylutens.Extremophiles : life under extreme conditions · 2020Article
- Equilibrium of the intracellular redox state for improving cell growth and L-lysine yield of Corynebacterium glutamicum by optimal cofactor swapping.Microbial cell factories · 2019Article
- Crystal Structure of the Isocitrate Dehydrogenase 2 from Acinetobacter baumannii (AbIDH2) Reveals a Novel Dimeric Structure with Two Monomeric-IDH-Like Subunits.International journal of molecular sciences · 2018Article
- Identification of osmoadaptive strategies in the halophile, heterotrophic ciliate Schmidingerothrix salinarum.PLoS biology · 2018Article
- Article
- Biochemical Characterization and Complete Conversion of Coenzyme Specificity of Isocitrate Dehydrogenase from Bifidobacterium longum.International journal of molecular sciences · 2016Article
- Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
NAD(+) use is an ancestral trait of isocitrate dehydrogenase (IDH), and the NADP(+) phenotype arose through evolution as an ancient adaptation event. However, no NAD(+)-specific IDHs have been found among type II IDHs and monomeric IDHs. In this study, novel type II homodimeric NAD-IDHs from Ostreococcus lucimarinus CCE9901 IDH (OlIDH) and Micromonas sp. RCC299 (MiIDH), and novel monomeric NAD-IDHs from Campylobacter sp. FOBRC14 IDH (CaIDH) and Campylobacter curvus (CcIDH) were reported for the first time. The homodimeric OlIDH and monomeric CaIDH were determined by size exclusion chromatography and MALDI-TOF/TOF mass spectrometry. All the four IDHs were demonstrated to be NAD(+)-specific, since OlIDH, MiIDH, CaIDH and CcIDH displayed 99-fold, 224-fold, 61-fold and 37-fold preferences for NAD(+) over NADP(+), respectively. The putative coenzyme discriminating amino acids (Asp326/Met327 in OlIDH, Leu584/Asp595 in CaIDH) were evaluated, and the coenzyme specificities of the two mutants, OlIDH R(326)H(327) and CaIDH H(584)R(595), were completely reversed from NAD(+) to NADP(+). The detailed biochemical properties, including optimal reaction pH and temperature, thermostability, and metal ion effects, of OlIDH and CaIDH were further investigated. The evolutionary connections among OlIDH, CaIDH, and all the other forms of IDHs were described and discussed thoroughly.
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