دورية أكاديمية
Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties
| العنوان: | Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties |
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| المؤلفون: | Brochier-Armanet, Céline, Madern, Dominique |
| المساهمون: | Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), ANR-16-CE11-0011,AlloAnc,Allostérie Ancestrale(2016) |
| المصدر: | ISSN: 0300-9084 ; Biochimie ; https://hal.univ-grenoble-alpes.fr/hal-03358405Test ; Biochimie, 2021, 191, pp.140-153. ⟨10.1016/j.biochi.2021.08.004⟩. |
| بيانات النشر: | HAL CCSD Elsevier |
| سنة النشر: | 2021 |
| المجموعة: | HAL Lyon 1 (University Claude Bernard Lyon 1) |
| مصطلحات موضوعية: | Allosteric regulation, Archaea, Lactate dehydrogenase, Malate dehydrogenase, Molecular evolution, Neofunctionalization, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] |
| الوصف: | International audience ; The NAD(P)-dependent malate dehydrogenases (MDH) (EC 1.1.1.37) and NAD-dependent lactate dehydrogenases (LDH) (EC. 1.1.1.27) form a large super-family that has been characterized in organisms belonging to the three Domains of Life. MDH catalyses the reversible conversion of the oxaloacetate into malate, while LDH operates at the late stage of glycolysis by converting pyruvate into lactate. Phylogenetic studies proposed that the LDH/MDH superfamily encompasses five main groups of enzymes. Here, starting from 16,052 reference proteomes, we reinvestigated the relationship between MDH and LDH. We showed that the LDH/MDH superfamily encompasses three main families: MDH1, MDH2, and a large family encompassing MDH3, LDH, and L-2-hydroxyisocaproate dehydrogenases (HicDH) sequences. An in-depth analysis of the phylogeny of the MDH3/LDH/HicDH family and of the nature of three important amino acids located within the catalytic site and involved in binding and substrate discrimination, revealed a large group of sequences displaying unexpected combinations of amino acids at these three critical positions. This group branched in-between MDH3 and LDH sequences. The functional characterization of several enzymes from this intermediate group disclosed a mix of functional properties, indicating that the MDH3/LDH/HicDH family is much more diverse than previously thought, and blurred the frontier between MDH3 and LDH enzymes. Present-days enzymes of the intermediate group are a valuable material to study the evolutionary steps that led to functional diversity and emergence of allosteric regulation within the LDH/MDH superfamily. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/34418486; hal-03358405; https://hal.univ-grenoble-alpes.fr/hal-03358405Test; https://hal.univ-grenoble-alpes.fr/hal-03358405/documentTest; https://hal.univ-grenoble-alpes.fr/hal-03358405/file/Armanet%20et%20al.%20Biochimie.pdfTest; PUBMED: 34418486 |
| DOI: | 10.1016/j.biochi.2021.08.004 |
| الإتاحة: | https://doi.org/10.1016/j.biochi.2021.08.004Test https://hal.univ-grenoble-alpes.fr/hal-03358405Test https://hal.univ-grenoble-alpes.fr/hal-03358405/documentTest https://hal.univ-grenoble-alpes.fr/hal-03358405/file/Armanet%20et%20al.%20Biochimie.pdfTest |
| حقوق: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.89E86A58 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.biochi.2021.08.004 |
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