The kinetic characteristics of human and trypanosomatid phosphofructokinases for the reverse reaction
| Autor: | James Kinkead, Paul A.M. Michels, Peter M Fernandes, Iain W. McNae, Frédéric Bringaud, Malcolm D. Walkinshaw |
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| Přispěvatelé: | Centre de résonance magnétique des systèmes biologiques (CRMSB), Centre National de la Recherche Scientifique (CNRS)-Université de Bordeaux (UB) |
| Rok vydání: | 2019 |
| Předmět: |
Gene isoform
Trypanosoma reverse reaction Trypanosoma cruzi Protozoan Proteins Phosphofructokinase Trypanosoma brucei [SDV.MP.PRO]Life Sciences [q-bio]/Microbiology and Parasitology/Protistology Biochemistry Glycosome 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Humans human Phosphofructokinases Molecular Biology Research Articles ComputingMilieux_MISCELLANEOUS 030304 developmental biology Leishmania chemistry.chemical_classification 0303 health sciences Trypanosomatid biology Chemistry Phosphotransferases Reverse reaction Fructose Cell Biology biology.organism_classification Isoenzymes Kinetics Cytosol Enzyme phosphofructokinase 030220 oncology & carcinogenesis Research Article Human |
| Zdroj: | Fernandes, P M, Kinkead, J R, McNae, I W, Michels, P A & Walkinshaw, M D 2019, ' The kinetic characteristics of human and trypanosomatid phosphofructokinases for the reverse reaction ', Biochemical Journal, vol. 476, no. 2, pp. 179-191 . https://doi.org/10.1042/BCJ20180635 Biochemical Journal Biochemical Journal, Portland Press, 2019, 476 (2), pp.179-191. ⟨10.1042/BCJ20180635⟩ |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | Eukaryotic ATP-dependent phosphofructokinases (PFKs) are often considered unidirectional enzymes catalysing the transfer of a phospho moiety from ATP to fructose 6-phosphate to produce ADP and fructose 1,6-bisphosphate. The reverse reaction is not generally considered to occur under normal conditions and has never been demonstrated for any eukaryotic ATP-dependent PFKs, though it does occur in inorganic pyrophosphate-dependent PFKs and has been experimentally shown for bacterial ATP-dependent PFKs. The evidence is provided via two orthogonal assays that all three human PFK isoforms can catalyse the reverse reaction in vitro, allowing determination of kinetic properties. Additionally, the reverse reaction was shown possible for PFKs from three clinically important trypanosomatids; these enzymes are contained within glycosomes in vivo. This compartmentalisation may facilitate reversal, given the potential for trypanosomatids to have an altered ATP/ADP ratio in glycosomes compared with the cytosol. The kinetic properties of each trypanosomatid PFK were determined, including the response to natural and artificial modulators of enzyme activity. The possible physiological relevance of the reverse reaction in trypanosomatid and human PFKs is discussed. |
| Databáze: | OpenAIRE |
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