ATP versus pyrophosphate: glycolysis revisited in parasitic protists

Mertens, Emmanuel

doi:10.1016/0169-4758(93)90169-g

Cited by 111 publications

(84 citation statements)

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“…The assumed significance of PP i as the phosphoryl donor is reflected in an increase of the ATP yield during glycolysis (16,26). This notion is supported by the predominant occurrence of PP i -PFK in organisms living in hypoxic or anoxic environments, which rely on anaerobic glycolysis (17).…”

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confidence: 48%

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family

et al. 2001

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Inorganic pyrophosphate-dependent phosphofructokinase (PP i -PFK) of the amitochondriate eukaryote Mastigamoeba balamuthi was sequenced and showed about 60% identity to PP i -PFKs from two eubacteria, Propionibacterium freudenreichii and Sinorhizobium meliloti. These gene products represent a newly recognized lineage of PFKs. All four lineages of group II PFKs, as defined by phylogenetic analysis, contained both prokaryotic and eukaryotic species, underlining the complex evolutionary history of this enzyme.We have recently extended our studies on glycolytic enzymes of parasitic amitochondriate eukaryotes (20) to the free-living Mastigamoeba balamuthi (ATCC 30984) (6) with the goal of comparing the metabolic properties of anaerobic and microaerophilic eukaryotes with dramatically different life styles. This species belongs to the pelobionts, a group of amitochondriate amoeboflagellate protists of uncertain evolutionary position (5, 25). We noted that the sequence of its phosphofructokinase (PFK) showed unexpected characteristics, prompting us to revisit the taxonomic distribution and relationships of various PFK types.Type A PFK, an enzyme of the glycolytic pathway, phosphorylates fructose 6-phosphate to fructose 1,6-bisphosphate. In most organisms, ATP is the phosphoryl donor (ATP-PFK; EC 2.7.1.11) of the irreversible reaction. A number of protists and plants and some eubacteria contain reversible PFKs, which use inorganic pyrophosphate (PP i ) instead of ATP (PP i -PFK; EC 2.7.1.90). The assumed significance of PP i as the phosphoryl donor is reflected in an increase of the ATP yield during glycolysis (16,26). This notion is supported by the predominant occurrence of PP i -PFK in organisms living in hypoxic or anoxic environments, which rely on anaerobic glycolysis (17).The evolutionary history of PFK does not coincide with accepted notions of organismic relationships and points to past gene duplications and lateral gene transfers. Based primarily on sequence characteristics, type A PFKs are currently assigned to three major groups (groups I, II, and III) (22). Group II can be further subdivided into four subgroups, which appear as robust clades in phylogenetic reconstructions (we are using the tentative nomenclature proposed for clades in group II [18]). Closely related organisms may contain close homologs of PFK which use different phosphoryl donors, indicating that enzyme specificity can change relatively easily (2), a conclusion recently confirmed experimentally (7). Some organisms even contain members of two such subgroups (8, 10-12). Phylogenetic analysis. Sequences of PP i -PFK homologs were retrieved from the National Center for Biotechnology Information protein database. The S. meliloti PFK sequence was retrieved from the website of the corresponding genome project (http://sequence.toulouse.inra.fr/meliloti.html) (3). Sequence sampling for group II encompasses the whole diversity present in the nonredundant National Center for Biotechnology Information database. Sampling of group III was restricted to ...

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confidence: 48%

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family

et al. 2001

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“…The PP i -dependent glycolytic enzymes, PPDK and phosphofructokinase (PP i -PFK), are expressed in a number of parasites to increase the energy efficiency of glycolysis. Indeed, the use of PP i as energy substrate increases the rate of ATP production from glucose 2.5-fold, assuming that PP i is a by-product of the biosynthetic reaction that is commonly wastefully hydrolyzed by pyrophosphatase activity (56). Thus, the trypanosome PPDK can theoretically produce 2 molecules of ATP/molecule of P-enolpyruvate consumed, if adenylate kinase (2 ADP 3 ATP ϩ AMP) and the absence of a glycosomal pyrophosphatase activity are integrated in the equation.…”

Section: Discussionmentioning

confidence: 99%

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Deramchia

Morand

Biran

et al. 2014

Journal of Biological Chemistry

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Background:The role of pyruvate phosphate dikinase (PPDK), which catalyzes a reversible reaction, is unknown in many eukaryotes. Results: Deletion of the trypanosomal PPDK gene affects glycolysis. Conclusion:In trypanosomes, PPDK works in the glycolytic direction and participates in the maintenance of the glycosomal ATP/ADP balance. Significance: The glycosomal PPDK provides a metabolic flexibility by producing 2 ATP per phosphoenolpyruvate consumed.

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“…The main differences are the presence of a GTP-dependent phosphoenolpyruvate carboxykinase (PEPCK) in the pyruvate kinase (PYK)/pyruvate:orthophosphate dikinase (PPDK) shunt (278) and the presence of an [Fe]-hydrogenase (287), homologous to the enzyme found in chytrids or trichomonads. As with Entamoeba, both PPDK and PYK activities are present at comparable levels (377), although the latter activity was long thought to be lacking (207,327). Also as with Entamoeba, the main end products are acetate and ethanol, usually a mixture of both, depending upon redox conditions: in the presence of small amounts of oxygen, the parasite utilizes diaph-…”

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confidence: 99%

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Müller

Mentel

Hellemond

et al. 2012

Microbiol Mol Biol Rev

687

925

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SUMMARY Major insights into the phylogenetic distribution, biochemistry, and evolutionary significance of organelles involved in ATP synthesis (energy metabolism) in eukaryotes that thrive in anaerobic environments for all or part of their life cycles have accrued in recent years. All known eukaryotic groups possess an organelle of mitochondrial origin, mapping the origin of mitochondria to the eukaryotic common ancestor, and genome sequence data are rapidly accumulating for eukaryotes that possess anaerobic mitochondria, hydrogenosomes, or mitosomes. Here we review the available biochemical data on the enzymes and pathways that eukaryotes use in anaerobic energy metabolism and summarize the metabolic end products that they generate in their anaerobic habitats, focusing on the biochemical roles that their mitochondria play in anaerobic ATP synthesis. We present metabolic maps of compartmentalized energy metabolism for 16 well-studied species. There are currently no enzymes of core anaerobic energy metabolism that are specific to any of the six eukaryotic supergroup lineages; genes present in one supergroup are also found in at least one other supergroup. The gene distribution across lineages thus reflects the presence of anaerobic energy metabolism in the eukaryote common ancestor and differential loss during the specialization of some lineages to oxic niches, just as oxphos capabilities have been differentially lost in specialization to anoxic niches and the parasitic life-style. Some facultative anaerobes have retained both aerobic and anaerobic pathways. Diversified eukaryotic lineages have retained the same enzymes of anaerobic ATP synthesis, in line with geochemical data indicating low environmental oxygen levels while eukaryotes arose and diversified.

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ATP versus pyrophosphate: glycolysis revisited in parasitic protists

Cited by 111 publications

References 34 publications

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

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ATP versus pyrophosphate: glycolysis revisited in parasitic protists

Cited by 111 publications

References 34 publications

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP i -Dependent Group II Phosphofructokinase Protein Family

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP i -Dependent Group II Phosphofructokinase Protein Family

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

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Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family

Presence of Prokaryotic and Eukaryotic Species in All Subgroups of the PP _i -Dependent Group II Phosphofructokinase Protein Family