Status: Bibliographieeintrag
Standort: ---
Exemplare:
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| Online-Ressource |
Verfasst von: | Urscher, Miriam [VerfasserIn]  |
| Alisch, Romy [VerfasserIn]  |
| Deponte, Marcel [VerfasserIn]  |
Titel: | The glyoxalase system of malaria parasites |
Titelzusatz: | implications for cell biology and general glyoxalase research |
Verf.angabe: | Miriam Urscher, Romy Alisch, Marcel Deponte |
E-Jahr: | 2011 |
Jahr: | 15 February 2011 |
Umfang: | 9 S. |
Fussnoten: | Gesehen am 01.12.2022 |
Titel Quelle: | Enthalten in: Seminars in cell & developmental biology |
Ort Quelle: | London : Academic Press, 1996 |
Jahr Quelle: | 2011 |
Band/Heft Quelle: | 22(2011), 3 vom: Mai, Seite 262-270 |
ISSN Quelle: | 1096-3634 |
Abstract: | Malaria parasites of the genus Plasmodium have developed sophisticated mechanisms to benefit from the nutrient-rich environments of their hosts. For example, by hiding in red blood cells, they found a secure way to tap into the glucose supply of vertebrates. The high-power metabolism of Plasmodium leads not only to a significantly increased glucose consumption of infected erythrocytes, but also to an elevated production of d-lactate from methylglyoxal. The latter substance is a harmful by-product from glycolysis that is detoxified by the ubiquitous glyoxalase system. This system consists of reduced glutathione and two enzymes, the glyoxalases 1 and 2. Inhibition of the glyoxalases in the host/parasite unit is expected to be highly detrimental to the parasite. Moreover, by studying Plasmodium isozymes, physiological functions of the system beyond methylglyoxal conversion became prima facie obvious: (i) the two different active sites of glyoxalase 1 as well as the existence of (insular) glyoxalases in the apicoplast point to alternative substrates and metabolic pathways. (ii) The allostery of glyoxlase 1 and the monomer-dimer equilibrium of glyoxalase 2 suggest novel regulatory features of these enzymes. Here we review the current knowledge on the glyoxalase systems of the host/parasite unit, discuss their potential as drug target and summarize new hypotheses on glyoxalases with respect to general cell biology. |
DOI: | doi:10.1016/j.semcdb.2011.02.003 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.semcdb.2011.02.003 |
| Volltext: https://www.sciencedirect.com/science/article/pii/S1084952111000164 |
| DOI: https://doi.org/10.1016/j.semcdb.2011.02.003 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Apicoplast |
| Enzyme catalysis |
| Glyoxalase |
| Malaria |
| Methylglyoxal |
K10plus-PPN: | 1824129157 |
Verknüpfungen: | → Zeitschrift |
¬The¬ glyoxalase system of malaria parasites / Urscher, Miriam [VerfasserIn]; 15 February 2011 (Online-Ressource)
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